Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.
Salts of hydrobromic acid, HBr, with the bromine atom in the 1- oxidation state. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.
Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
The sum of the weight of all the atoms in a molecule.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).
A trypanocidal agent and possible antiviral agent that is widely used in experimental cell biology and biochemistry. Ethidium has several experimentally useful properties including binding to nucleic acids, noncompetitive inhibition of nicotinic acetylcholine receptors, and fluorescence among others. It is most commonly used as the bromide.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
An enzyme catalyzing the transfer of a phosphate group from 3-phospho-D-glycerate in the presence of ATP to yield 3-phospho-D-glyceroyl phosphate and ADP. EC 2.7.2.3.
Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
A paralytic condition of the legs caused by ingestion of lathyrogens, especially BETA-AMINOPROPIONITRILE or beta-N-oxalyl amino-L-alanine, which are found in the seeds of plants of the genus LATHYRUS.
Biologically active molecules which are covalently bound to the enzymes or binding proteins normally acting on them. Binding occurs due to activation of the label by ultraviolet light. These labels are used primarily to identify binding sites on proteins.
A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
A muscarinic antagonist structurally related to ATROPINE but often considered safer and more effective for inhalation use. It is used for various bronchial disorders, in rhinitis, and as an antiarrhythmic.
Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A sulfur-containing essential L-amino acid that is important in many body functions.
A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.
Sites on an antigen that interact with specific antibodies.
A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Benzoic acid esters or salts substituted with one or more iodine atoms.
A colorless inorganic compound (HONH2) used in organic synthesis and as a reducing agent, due to its ability to donate nitric oxide.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrates are composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Contractile tissue that produces movement in animals.
The rate dynamics in chemical or physical systems.
A system of universal human blood group isoantigens with many associated subgroups. The M and N traits are codominant and the S and s traits are probably very closely linked alleles, including the U antigen. This system is most frequently used in paternity studies.
Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.
Organic compounds that contain the (-NH2OH) radical.
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An electrochemical process in which macromolecules or colloidal particles with a net electric charge migrate in a solution under the influence of an electric current.
The process of cleaving a chemical compound by the addition of a molecule of water.
A brominating agent that replaces hydrogen atoms in benzylic or allylic positions. It is used in the oxidation of secondary alcohols to ketones and in controlled low-energy brominations. (From Miall's Dictionary of Chemistry, 5th ed; Hawley's Condensed Chemical Dictionary, 12th ed,).
Analogs and derivatives of atropine.
COLLAGEN DISEASES characterized by brittle, osteoporotic, and easily fractured bones. It may also present with blue sclerae, loose joints, and imperfect dentin formation. Most types are autosomal dominant and are associated with mutations in COLLAGEN TYPE I.
Antimuscarinic quaternary ammonium derivative of scopolamine used to treat cramps in gastrointestinal, urinary, uterine, and biliary tracts, and to facilitate radiologic visualization of the gastrointestinal tract.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.
Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An analytical technique for resolution of a chemical mixture into its component compounds. Compounds are separated on an adsorbent paper (stationary phase) by their varied degree of solubility/mobility in the eluting solvent (mobile phase).
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
A ZINC-dependent carboxypeptidase primary found in the DIGESTIVE SYSTEM. The enzyme catalyzes the preferential cleavage of a C-terminal peptidyl-L-lysine or arginine. It was formerly classified as EC 3.4.2.2 and EC 3.4.12.3.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
A genus of ascomycetous fungi, family Sordariaceae, order SORDARIALES, comprising bread molds. They are capable of converting tryptophan to nicotinic acid and are used extensively in genetic and enzyme research. (Dorland, 27th ed)
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A method of gel filtration chromatography using agarose, the non-ionic component of agar, for the separation of compounds with molecular weights up to several million.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
An essential amino acid. It is often added to animal feed.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.

The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis. (1/1543)

Serum amyloid A isoforms, apoSAA1 and apoSAA2, are apolipoproteins of unknown function that become major components of high density lipoprotein (HDL) during the acute phase of an inflammatory response. ApoSAA is also the precursor of inflammation-associated amyloid, and there is strong evidence that the formation of inflammation-associated and other types of amyloid is promoted by heparan sulfate (HS). Data presented herein demonstrate that both mouse and human apoSAA contain binding sites that are specific for heparin and HS, with no binding for the other major glycosaminoglycans detected. Cyanogen bromide-generated peptides of mouse apoSAA1 and apoSAA2 were screened for heparin binding activity. Two peptides, an apoSAA1-derived 80-mer (residues 24-103) and a smaller carboxyl-terminal 27-mer peptide of apoSAA2 (residues 77-103), were retained by a heparin column. A synthetic peptide corresponding to the CNBr-generated 27-mer also bound heparin, and by substituting or deleting one or more of its six basic residues (Arg-83, His-84, Arg-86, Lys-89, Arg-95, and Lys-102), their relative importance for heparin and HS binding was determined. The Lys-102 residue appeared to be required only for HS binding. The residues Arg-86, Lys-89, Arg-95, and Lys-102 are phylogenetically conserved suggesting that the heparin/HS binding activity may be an important aspect of the function of apoSAA. HS linked by its carboxyl groups to an Affi-Gel column or treated with carbodiimide to block its carboxyl groups lost the ability to bind apoSAA. HDL-apoSAA did not bind to heparin; however, it did bind to HS, an interaction to which apoA-I contributed. Results from binding experiments with Congo Red-Sepharose 4B columns support the conclusions of a recent structural study which found that heparin binding domains have a common spatial distance of about 20 A between their two outer basic residues. Our present work provides direct evidence that apoSAA can associate with HS (and heparin) and that the occupation of its binding site by HS, and HS analogs, likely caused the previously reported increase in amyloidogenic conformation (beta-sheet) of apoSAA2 (McCubbin, W. D., Kay, C. M., Narindrasorasak, S., and Kisilevsky, R. (1988) Biochem. J. 256, 775-783) and their amyloid-suppressing effects in vivo (Kisilevsky, R., Lemieux, L. J., Fraser, P. E., Kong, X., Hultin, P. G., and Szarek, W. A. (1995) Nat. Med. 1, 143-147), respectively.  (+info)

The amino acid sequence of rabbit cardiac troponin I. (2/1543)

The complete amino acid sequence of troponin I from rabbit cardiac muscle was determined by the isolation of four unique CNBr fragments, together with overlapping tryptic peptides containing radioactive methionine residues. Overlap data for residues 35-36, 93-94 and 140-145 are incomplete, the sequence at these positions being based on homology with the sequence of the fast-skeletal-muscle protein. Cardiac troponin I is a single polypeptide chain of 206 residues with mol.wt. 23550 and an extinction coefficient, E 1%,1cm/280, of 4.37. The protein has a net positive charge of 14 and is thus somewhat more basic than troponin I from fast-skeletal muscle. Comparison of the sequences of troponin I from cardiac and fast skeletal muscle show that the cardiac protein has 26 extra residues at the N-terminus which account for the larger size of the protein. In the remainder of sequence there is a considerable degree of homology, this being greater in the C-terminal two-thirds of the molecule. The region in the cardiac protein corresponding to the peptide with inhibitory activity from the fast-skeletal-muscle protein is very similar and it seems unlikely that this is the cause of the difference in inhibitory activity between the two proteins. The region responsible for binding troponin C, however, possesses a lower degree of homology. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50072 (20 pages), at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1976) 153, 5.  (+info)

The primary structure of the parvalbumin II of pike (Esox lucius). (3/1543)

The amino acid sequence of the parvalbumin II of the pike is reported. The protein has a molecular weight of 11 435. It consists of a single polypeptide chain of 107 amino acid residues with an acetyl group blocking the N-terminus and an alanine residue at the C-terminus. The molecule has been enzymically cleaved by trypsin, thermolysin and by the protease of the Staphylococcus aureus strain V8. Chemical cleavages make use of the CNBr reaction and of the sulfocyanoethylation method. The comparison of this amino acid sequence with that of the parvalbumin III of the pike indicates that these two homologous proteins belong respectively to two different subgroups derived from an early gene duplication of an ancestral gene at least prior to the differentiation of the Osteichthyes.  (+info)

Thermodynamic and kinetic analysis of the Escherichia coli thioredoxin-C' fragment complementation system. (4/1543)

Escherichia coli thioredoxin was cleaved with CNBr at its single Met residue at position 37, which lies in the middle of a long alpha-helix. The two fragments, 1-37 and 38-108, were purified and characterized by using CD and fluorescence spectroscopy. Both fragments lack structure at neutral pH and room temperature. The secondary and tertiary structural contents of the non-covalent complex formed on the mixing of the two peptide fragments are 47% and 35% of the intact protein respectively. The thermodynamics and kinetics of fragment association were characterized by titration calorimetry and stopped-flow fluorescence spectroscopy. Single phases were observed for both association and dissociation, with rate constants at 298 K of kon=4971+/-160 M-1.s -1 and koff=0. 063+/-0.009 s-1 respectively. The ratio kon/koff was very similar to the binding constant determined by titration calorimetry, suggesting that binding is a two-state process. The values for DeltaCp, DeltaH0 and DeltaG0 at 298 K for dissociation of the complex were 5.7 kJ. mol-1.K-1, 45.3 kJ.mol-1 and 29.8 kJ.mol-1 respectively. The value for DeltaH0 was linearly dependent on temperature from 8-40 degrees C, suggesting that DeltaCp is independent of temperature. The values for DeltaCp and DeltaG0 are very similar to the corresponding values for the unfolding of intact thioredoxin at 25 degrees C. However, both DeltaH0 and DeltaS are significantly more positive for dissociation of the complex, suggesting a decreased hydrophobic stabilization of the complex relative to the situation for intact thioredoxin.  (+info)

Oxidative refolding of recombinant prochymosin. (5/1543)

The disulphide-coupled refolding of recombinant prochymosin from Escherichia coli inclusion bodies was investigated. Prochymosin solubilized from inclusion bodies is endowed with free thiol groups and disulphide bonds. This partially reduced form undergoes renaturation more efficiently than the fully reduced form, suggesting that some native structural elements existing in inclusion bodies and remaining after denaturation function as nuclei to initiate correct refolding. This assumption is supported by the finding that in the solubilized prochymosin molecule the cysteine residues located in the N-terminal domain of the protein are not incorrectly paired with the other cysteines in the C-terminal domain. Addition of GSH/GSSG into the refolding system facilitates disulphide rearrangement and thus enhances renaturation, especially for the fully reduced prochymosin. Based on the results described in this and previous papers [Tang, Zhang and Yang (1994) Biochem. J. 301, 17-20], a model to depict the refolding process of prochymosin is proposed. Briefly, the refolding process of prochymosin consists of two stages: the formation and rearrangement of disulphide bonds occurs at the first stage in a pH11 buffer, whereas the formation and adjustment of tertiary structure leading to the native conformation takes place at the second stage at pH8. The pH11 conditions help polypeptides to refold in such a way as to favour the formation of native disulphide bonds. Disulphide rearrangement, the rate-limiting step during refolding, can be achieved by thiol/disulphide exchange initiated by free thiol groups present in the prochymosin polypeptide, GSH/GSSG or protein disulphide isomerase.  (+info)

Characterization of the myosin light chain kinase from smooth muscle as an actin-binding protein that assembles actin filaments in vitro. (6/1543)

In addition to its kinase activity, myosin light chain kinase has an actin-binding activity, which results in bundling of actin filaments [Hayakawa et al., Biochem. Biophys. Res. Commun. 199, 786-791, 1994]. There are two actin-binding sites on the kinase: calcium- and calmodulin-sensitive and insensitive sites [Ye et al., J. Biol. Chem. 272, 32182-32189, 1997]. The calcium/calmodulin-sensitive, actin-binding site is located at Asp2-Pro41 and the insensitive site is at Ser138-Met213. The cyanogen bromide fragment, consisting of Asp2-Met213, is furnished with both sites and is the actin-binding core of myosin light chain kinase. Cross-linking between the two sites assembles actin filaments into bundles. Breaking of actin-binding at the calcium/calmodulin-sensitive site by calcium/calmodulin disassembles the bundles.  (+info)

A study of renaturation of reduced hen egg white lysozyme. Enzymically active intermediates formed during oxidation of the reduced protein. (7/1543)

The material obtained from reduced hen egg white lysozyme after complete air oxidation at pH 8.0 and 37 degrees has yielded, by gel filtration on a Bio-Gel P-30 column, enzymically active species and an enzymically inactive form which eluted sooner than the active species but later than expected for a dimer of lysozyme. Reduced lysozyme also elutes at the same position as this inactive material. Examination of the fragments produced on CNBr cleavage of the inactive form indicates that at least 24% of the population contains incorrect disulfide bonds involving half-cystine residues 6, 30, 115, and 127. Tryptophan fluorescence and the intrinsic viscosity of the inactive form show an enlarged molecular domain with a disordered conformation. The yield of the inactive form increases as the oxidation of reduced lysozyme is accelerated using cupric ion. In the presence of 4 X 10(-5) M cupric ion, reduced lysozyme forms almost quantitatively the inactive form, which is almost completely converted to the native form by sulfhydryl-disulfide interchange catalyzed by thiol groups of either reduced lysozyme or beta-mercaptoethanol. The material trapped by alkylation of the free sulfhydryl groups with [1-14C]iodoacetic acid during the early stage of air oxidation of reduced lysozyme was fractionated by gel filtration to permit separation of the active species from the inactive form. Ion exchange chromatography of the active species yielded completely renatured lysozyme and three major enzymically active radioactive derivatives. Two of these derivatives contained approximately 2 mol of S-carboxymethylcysteine. Isolation and characterization of radioactive tryptic peptides from each of the three active forms, permitted the identification of Cys 6 and Cys 127, Cys 76 and 94, and Cys 80 as the sulfhydryl groups alkylated in these three incompletely oxidized, partially active forms. Thus, it appears that the interatomic interactions maintaining the compact three-dimensional structure of native lysozyme are operational even when one of these three native disulfide bonds between Cys 6 and Cys 127, Cys 76 and Cys 94, and Cys 64 and 80 is open.  (+info)

Hydrophobic photolabeling as a new method for structural characterization of molten globule and related protein folding intermediates. (8/1543)

Recent advances in attempts to unravel the protein folding mechanism have indicated the need to identify the folding intermediates. Despite their transient nature, in a number of cases it has been possible to detect and characterize some of the equilibrium intermediates, for example, the molten globule (MG) state. The key features of the MG state are retention of substantial secondary structure of the native state, considerable loss of tertiary structure leading to increased hydrophobic exposure, and a compact structure. NMR, circular dichroism, and fluorescence spectroscopies have been most useful in characterizing such intermediates. We report here a new method for structural characterization of the MG state that involves probing the exposed hydrophobic sites with a hydrophobic photoactivable reagent--2[3H]diazofluorene. This carbene-based reagent binds to hydrophobic sites, and on photolysis covalently attaches itself to the neighboring amino acid side chains. The reagent photolabels alpha-lactalbumin as a function of pH (3-7.4), the labeling at neutral pH being negligible and maximal at pH 3. Chemical and proteolytic fragmentation of the photolabeled protein followed by peptide sequencing permitted identification of the labeled residues. The results obtained indicate that the sequence corresponding to B (23-34) and C (86-98) helix of the native structure are extensively labeled. The small beta-domain (40-50) is poorly labeled, Val42 being the only residue that is significantly labeled. Our data, like NMR data, indicate that in the MG state of alpha-lactalbumin, the alpha-domain has a greater degree of persistent structure than the beta-domain. However, unlike the NMR method, the photolabeling method is not limited by the size of the protein and can provide information on several new residues, for example, Leu115. The current method using DAF thus allows identification of stable and hydrophobic exposed regions in folding intermediates as the reagent binds and on photolysis covalently links to these regions.  (+info)

I am planning on doing a cyanogen bromide digest of huamn serum albumin next week and I was looking for some pointers from anyone with CNBr digest experience. 1. The method I found calls for dissolving the protein in 70% formic acid, adding solid CNBr (2 mg CNBr/mg protein), and then letting react for 24h at RT in the dark. Is this a reliable and efficient procedure? 2. If I try the CNBr digest on HSA without first reducing the disulfides, will the CNBr cleave or modify the disulfides? 3. If I do reduce the disulfides of HSA but do not alkylate before the CNBr digest, will the cysteines end up alkylated (to the isothiocyanate)? Any help would be appreciated! -David ...
Studies were made to characterise soluble Alfa-Amylase (Bacterial). The kinetics of Alfa-amylase on starch is zero order at room temperature (28 0 c) for the first 5 minutes. Hence the activity of Alfa-amylase was measured in terms of mg maltose released during first five minutes. Alfa-amylase showed optimal activity at pH 6.0 Cyanogen bromide was prepared and was used to activate sephadex G200 at pH 11.5. The volume of the cyanogen bromide activated gel, at this pH decreased by about 50 percent, compared to that of the unactivated Sephadex G200. Alfa-amylase was coupled to cyanogen bromide activated Sephadex G200 at pH8.3 and 7.0. Coupling of the enzyme led to further decrease in volumes of about 15 percent and 6 percent at pH 8.3 and 7.0 respectively. The amounts of protein in the immobilized Alfa-amylase prepared at pH 8.3 and 7.0 were estimated by, Kjeldhal method, by the tryptophan content and from the difference in the amount of protein present in the original solution and that in the ...
Lookchem Provide Cas No.506-68-3 Basic information: Properties,Safety Data,Sds and Other Datebase. We also Provide Trading Suppliers & Manufacture for 506-68-3 Cyanogen bromide.
The National Institute of Standards and Technology (NIST) uses its best efforts to deliver a high quality copy of the Database and to verify that the data contained therein have been selected on the basis of sound scientific judgment. However, NIST makes no warranties to that effect, and NIST shall not be liable for any damage that may result from errors or omissions in the Database ...
We couldnt find a conversion between grams Cyanogen Chloride and nanomol Do a quick conversion: 1 grams Cyanogen Chloride = 1 nanomol using the online calculator for metric conversions.
Absolute spectrophotometry of the coma of Comet Kohoutek 1973f is discussed for the nights of January 24 and 26, 1974. Specific intensities are measured for spectral features and a continuum band in the wavelength region λλ3460-6062Å. The (0, 0) band of the ∆ν = 0 sequence of the violet system of the cyanogen molecule is analyzed and column densities of 1.7 × 10 |SUP|15|/SUP|m |SUP|-2|/SUP| and 3.4 × 10 |SUP|14|/SUP|m |SUP|-2|/SUP| are found for January 24 and 26, 1974, respectively. The analysis of the bands of C|SUB|2|/SUB| will be reported in a second paper of this series.
It is not difficult to immobilize a protein on a solid support using any classic activation method such as the cyanogen bromide or N-hydroxysuccinimidylcarboxylate... However, if the protein of interest is a specific antibody, its biological activity will be affected if not entirely lost after the covalent linkage between the solid support with the active site H2N of the antibody.. AFFILAND has developed an Antibody Activated Binding Gel for immobilizing the antibody at its Fc portion leaving free its Fab. The biological properties of immobilized antibody will be so conserved.. II. PURIFICATION OF ANTIGEN BY CORRESPONDING IMMUNOAFFINITY COLUMN ...
It is not difficult to immobilize a protein on a solid support using any classic activation method such as the cyanogen bromide or N-hydroxysuccinimidylcarboxylate... However, if the protein of interest is a specific antibody, its biological activity will be affected if not entirely lost after the covalent linkage between the solid support with the active site H2N of the antibody.. AFFILAND has developed an Antibody Activated Binding Gel for immobilizing the antibody at its Fc portion leaving free its Fab. The biological properties of immobilized antibody will be so conserved.. II. PURIFICATION OF ANTIGEN BY CORRESPONDING IMMUNOAFFINITY COLUMN ...
TY - JOUR. T1 - Characterization of the cyanogen bromide fragments of the β chain of human haptoglobin. AU - Kurosky, Alexander. AU - Hay, Regine E.. AU - Kim, Han Hwa. AU - Touchstone, Billy. AU - Rasco, Marilyn A.. AU - Bowman, Barbara H.. PY - 1976. Y1 - 1976. N2 - Characterization of the cyanogen bromide (CNBr) fragments of the β chain of human haptoglobin revealed five major fragments resulting from cleavage of four methionyl residues. The fragments were isolated by gel filtration in guanidine-HCl on Sepharose 6B and Bio-Gel P10 and P60. Compositional analyses of the five cyanogen bromide fragments accounted for 248-253 amino acid residues in agreement with the number of residues determined for the intact β chain. Most of the carbohydrate was attached to CNBr II. Automated amino-terminal sequence analysis and carboxyl-terminal hydrolysis with carboxypeptidase of the haptoglobin β chain and cyanogen bromide fragments identified 139 residues, or about 55% of the β-chain molecule. The ...
Cyanogen was first synthesized in 1815 by Joseph Louis Gay-Lussac, who determined its empirical formula and named it. Gay-Lussac coined the word cyanogène from the Greek words κυανός (kyanos, blue) and γεννάω (gennao, I create), because cyanide was first isolated by the Swedish chemist Carl Wilhelm Scheele from the pigment Prussian blue.[14] By the 1850s, cyanogen soap was used by photographers to remove silver stains from their hands.[15] It attained importance with the growth of the fertilizer industry in the late 19th century and remains an important intermediate in the production of many fertilizers. It is also used as a stabilizer in the production of nitrocellulose. In 1910 a spectroscopic analysis of Halleys Comet found cyanogen in the comets tail, which led to public fear that the Earth would be poisoned as it passed through the tail. Because of the extremely diffuse nature of the tail, there was no effect when the planet passed through it.[16][17]. ...
TY - JOUR. T1 - Implementation of new TPD analysis techniques in the evaluation of second order desorption kinetics of cyanogen from Cu(001). AU - Ciftlikli, Erkan Z.. AU - Lee, Everett Y.M.. AU - Lallo, James. AU - Rangan, Sylvie. AU - Senanayake, Sanjaya D.. AU - Hinch, B. J.. PY - 2010/12/21. Y1 - 2010/12/21. N2 - The interactions of cyanide species with a copper (001) surface were studied with temperature programmed desorption (TPD) and X-ray photoelectron spectroscopy (XPS). Adsorbed cyanide species (CN(a)) undergo recombinative desorption evolving molecular cyanogen (C2N 2). As the adsorbed CN species charge upon adsorption, mutually repulsive dipolar interactions lead to a marked desorption energy reduction with increasing CN(a) coverages. Two new TPD analysis approaches were developed, which used only accurately discernible observables and which do not assume constant desorption energies, Ed, and pre-exponential values, ν. These two approaches demonstrated a linear variation of Ed with ...
Cyanogen bromide (CNBr) is the most common method for preparing affinity chromatography to purify antibody because of its simplicity and mild pH conditions. CNBr reacts with the hydroxyl groups on agarose to form cyanate esters and imidocarbonates. These groups are reacted with primary amines in order to couple the protein onto the agarose matrix. - Antibody Purification (Affinity) - AbVideo™ - Support - Abnova
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OnePlus seems to be having one heck of a brutal week since it announced the India launch of OnePlus One with Amazon next week. Cyanogen Inc ...
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Aldrich-53272; Hexyltrimethylammonium bromide |=98.0% (AT); CAS Number: 2650-53-5; Linear Formula: CH3(CH2)5N(Br)(CH3)3; find related products, papers, technical documents, MSDS & more at Sigma-Aldrich.
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The amino acid sequence of the alpha-subunit of taipoxin, an extremely potent presynaptic neurotoxin from the Australian snake taipan has been determined. The very basic protein, by itself a moderately neurotoxic phospholipase, consists of a single polypeptide chain of 119 amino acids. The main fragmentation of the reduced and S-carboxymethylated derivative was accomplished by cleavage with Staphylococcus aureus V8 protease and trypsin. Chymotryptic peptides and cyanogen bromide fragments were used to align and complete the sequence, which was determined by automated Edman degradation. The taipoxin alpha-subunit is closely homologous to the other taipoxin subunits and to other elapid snake venom phospholipases A2.
Complete amino acid sequences were determined for thymopoietins I and II (revision), isolated from bovine thymus, and for thymopoietin III, a newly identified polypeptide isolated from bovine spleen. Thymopoietin III (TP-III) is a 49 amino acid monomeric peptide that shows minor microheterogeneity at residue 34. The three thymopoietins have largely identical sequences yet some distinct differences, suggesting very recent evolution from a common gene. The complete amino acid sequences are (Formula: see text). ...
In article ,CKBILy.7pG at ucdavis.edu, szsclark at hamlet.ucdavis.edu (Sonya Clark) writes: ,Dear Netters - I am purifying antibodies from a polyclonal prep by ,running them over a CNBr-activated Sepharose affinity column of my ,antigen. As CNBr-activated Sepharose is expensive &/or horrible to make, Well it isnt that expensive compared to the time saved by buying it (unless youre a graduate student whose time isnt valued much) and it isnt all that bad to make (N-methyl-pyrrolidone/Na2CO3 method ) if you have a fume hood but anyhow ,Id like to strip the column of the antigen currently bound, and re-use ,the sepharose to make another affinity column. the real point is that the activated bond from the CNBr is used up by the coupling procedure. Even if you could get the protein off, youre back to unactivated sepharose. Joe Mack mack at ncifcrf.gov Does anyone have a protocol ,to do this? Would eluting the column with harsh eluents (eg. ,Guanidine/urea/SDS) work? and would I then be able to ...
Cellular responses of adhesion, spreading, or migration to adhesive GPs are mediated by multiple recognition domains of individual molecules.33 35 Many adhesive GPs involved in cell-cell and cell-matrix interactions, including fibrin(ogen), have both HBDs8 9 10 11 12 13 14 15 16 17 18 and RGD cell binding domains.32 33 34 36 37 38 39 Therefore, fibrin solubilized by CNBr cleavage was used to explore the structural requirements of binding to cultured EC monolayers and to study the potential involvement of both RGDS- and heparin-mediated interactions in this binding. Because the coiled-coil region imparts structural rigidity to fibrin(ogen) molecules,40 we postulated that limited cleavage within this region would aid in retention of the conformational integrity of the cryptic β15-42 HBD.18 Therefore, partial CNBr cleavage of methionine residues was performed to produce large-molecular-weight but soluble fragments of fibrin (Fig 2⇑). ELISA and Western blot analysis of CNBr fragments of FBG and ...
Cyanogen halides are employed for binding water-soluble proteins and water-soluble peptides containing a primary or secondary amino group to a water-insoluble polymer containing one or more hydroxyl and/or primary and/or secondary amino groups. The invention is useful, among other things, for binding watersoluble enzymes to water-insoluble polymers while preserving the activity of the enzyme.
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CAS NO:896465-66-0; Chemical name:1-Isoamyl-2-methyl-3,3-dibenzyl-5-chloroindolium bromide ; physical and chemical property of 896465-66-0, 1-Isoamyl-2-methyl-3,3-dibenzyl-5-chloroindolium bromide is provided by ChemNet.com
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Optimized PM6_D3H4 data set: MERS=(1,2,1) GNORM=4 PM6-D3H4 THREADS=1 Titanium(iv) bromide (TiBr4) (PM6-D3H4) Ti 0.42698700 +1 0.2117731 +1 0.8921759 +1 Ti -4.30491892 +1 -6.4773070 +1 -1.5004360 +1 Ti 0.29021966 +1 -0.9009843 +1 -4.2307153 +1 Br -3.69888946 +1 -1.8617788 +1 -7.1002692 +1 Br -1.83235907 +1 0.6018724 +1 1.8313998 +1 Br -6.38944936 +1 -2.5674896 +1 1.9787709 +1 Br 1.33312170 +1 -2.1289795 +1 -6.6325740 +1 Br -4.52669224 +1 -1.2562574 +1 -4.8394398 +1 Br 0.38164887 +1 2.5009449 +1 -0.5997460 +1 Br -2.95861573 +1 -8.5301858 +1 -0.6240677 +1 Br -1.81455526 +1 -2.2341104 +1 -3.7158022 +1 Br -1.96759876 +1 -4.9482290 +1 -2.3612729 +1 Br -0.93164843 +1 -0.0371416 +1 -1.6955077 +1 Br -4.34518515 +1 -2.7016668 +1 -1.9973386 +1 Br 1.63487108 +1 -0.1297490 +1 -1.5933006 +1 Br -6.60795364 +1 -3.6162984 +1 -4.6166030 +1 Br 3.06474099 +1 0.2288122 +1 1.4148497 +1 Br -2.55751279 +1 -5.1568974 +1 0.0759385 +1 Br -0.79366532 +1 0.7826121 +1 -6.3379464 +1 Ti -3.72372204 +1 -3.8230296 +1 -4.4825364 ...
TY - JOUR. T1 - Microsequencing of dopamine beta-monooxygenase. AU - McCafferty, B.. AU - Angeletti, R. H.. PY - 1987. Y1 - 1987. N2 - Tryptic peptides and cyanogen bromide fragments of dopamine beta-monooxygenase (DBH) were prepared and separated on C-8 reverse phase columns by high pressure liquid chromatography. Absorbance profiles at both 220 nm and 280 nm were monitored so that peptides with aromatic residues could be isolated. These peptides were subjected to automated Edmann degradation with a gas phase microsequencer.. AB - Tryptic peptides and cyanogen bromide fragments of dopamine beta-monooxygenase (DBH) were prepared and separated on C-8 reverse phase columns by high pressure liquid chromatography. Absorbance profiles at both 220 nm and 280 nm were monitored so that peptides with aromatic residues could be isolated. These peptides were subjected to automated Edmann degradation with a gas phase microsequencer.. UR - ...
TY - JOUR. T1 - alpha-chain sequence of newt haemoglobin (Taricha granulosa).. AU - Coates, M.. AU - Brimhall, B.. AU - Stenzel, Peter. AU - Hermodson, M.. AU - Gibson, D.. AU - Jones, R. T.. AU - Vedvick, T.. PY - 1977/4. Y1 - 1977/4. N2 - The amino acid sequence of the alpha-chain of the major haemoglobin of a newt, T. granulosa, has been determined. The chain is 142 residues long and has an extra methionine at its N-terminus when compared with human alpha-chain. Most of the tryptic peptides were sequenced by a combination of the subtractive Edman method and by deduction from the compositions of overlapping fragments produced by various enzymic treatments. The sequence of two core regions was obtained by automatic sequencing of large peptides produced by trypsin cleavage at arginine residues only after blockage of lysine residues by citraconylation; by cleavage between aspartic acid and proline residues with 70% formic acid, and by cyanogen bromide cleavage at methionine residues. The ...
United States Patent Inventors William S. Durrell; Robert J. Eckert, ,Ir., both of Mobile, Ala. 751,197 Aug. 8, 1968 July 20, 197 1 Gelgy Chemical Corporation Ardsley, N.Y. Appl. No. Filed Patented Assignee PROCESS FOR THE SEPARATION OF GASEOUS MIXTURES OF CYANOGEN CHLORIDE AND HYDROGEN CHLORIDE 6 Claims, 1 Drawing Fig. U.S. Cl 55/51, 55/71, 55/94, 23/15 1 23/154 Int. CL B0ld 53/14 FieldofSearch 55/71,93, [56] References Cited UNITED STATES PATENTS 2,220,570 11/1940 l-lurt 55/71 2,730,194 1/1956 Wohlers etal 55/71 X 2,826,546 3/1958 Walpert et al. 55/71 X 3,197,273 /1965 Trickey 23/14 3,242,647 3/1966 Alkemade et al 5 5/71 Primary Examiner.lohn Adee Attorneys-Karl F. Jorda, Bruce M. Collins, Martin J. Spellman, Jr. and Nestor W. Shust BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to the separation of hydrogen chloride from gaseous mixtures of the same with cyanogen chloride, formed as an intermediate in the heretofore known synthesis of cyanuric chloride. ...
The amino acid sequence of fragments obtained by cyanogen bromide cleavage of the mu-chain of a human γM-globulin is homologous to the NH2-terminal sequences of the gamma-chain of human and rabbit γG-globulins and is related to that of human light chains. This supports the hypothesis that light and heavy chains evolved from a common ancestral gene. ...
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5. A process for preparing compounds of the formula (I), as defined in claim 1, in which R1 represents hydrogen, characterized in that a compound of the formula (II) ##STR00198## in which A and Z have the meanings given in claim 1 andR8 represents hydrogen, methyl or ethyl,is initially converted, with activation of the ester or the carboxylic acid function with a compound of the formula (III) ##STR00199## in which n, R2 and R3 have the meanings given in claim 1andPG represents a hydroxyl protective group,into a compound of the formula (IV) ##STR00200## in which n, A, PG, Z, R2 and R3 have the meanings given in claim 1, then either[A] by removal of the protective group PG converted into a compound of the formula (V) ##STR00201## in which n, A, Z, R2 and R3 have the meanings given in claim 1,and the compound of the formula (V) is then in the presence of an acid converted with cyanogen bromide into a compound of the formula (I-A) ##STR00202## in which n, A, Z, R2 and R3 have the meanings given in ...
Thehemolysateofthe AntarcticteleostGobionotothen gibberifrons(family Nototheniidae) contains two hemoglo-bins (Hb 1 andHb 2). The concentration of Hb 2 (15-20% of the total hemoglobin content) is higher than that found in most cold-adapted Notothenioidei. Unlike the other Antarctic species so far examined having two hemoglobins, Hb 1 and Hb 2 do not have globin chains in common. Therefore this hemoglobin system is made of four globins (two a-and twob-chains). The complete amino-acid sequence of the two hemoglobins (Hb 1,a 1 2b 1 2 ;Hb 2,a 2 b 2 2 ) has been established. ... ...
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|p |Silia|em||span style=color: #f37021;|Bond|/span||/em||sup|®|/sup| Propyl Bromide (Si-PBR) is a versatile solid support for amines and alcohols. It is more reactive than the chloride towards displacement.|/p| |p||a href={{media url=specshe
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Cyanogen chloride and cyanogen bromide each trimerize at elevated temperatures over a carbon catalyst. The chloride gives ... Morris, Joel; Kovács, Lajos; Ohe, Kouichi (2015). "Cyanogen Bromide". Encyclopedia of Reagents for Organic Synthesis. pp. 1-8. ... Joel Morris; Lajos Kovács (2008). "Cyanogen Bromide". Encyclopedia of Reagents for Organic Synthesis. doi:10.1002/047084289X. ... Like the chloride, it undergoes ab exothermic trimerisation to form cyanuric bromide. This reaction is catalyzed by traces of ...
Cyanogen bromide - CNBr. *Cyanogen chloride - CNCl. *Cyanogen iodide - ICN. *Cyanogen - (CN)2 ...
Characterization of disulfide-containing cyanogen-bromide fragments". Eur. J. Biochem. 77 (3): 595-610. doi:10.1111/j.1432- ...
Cyanogen bromide peptides and complete amino acid sequence". J. Biol. Chem. 255 (13): 6412-20. PMID 7391027. Fujii H, Krietsch ...
I. Amino acid sequence of the cyanogen bromide peptides". The Journal of Biological Chemistry. 255 (7): 2878-85. PMID 6987229. ...
Cyanogen bromide cleavage and N-terminal sequences of the fragments". The Biochemical Journal. 215 (3): 565-71. doi:10.1042/ ...
By cleavage (tertiary amines only) with cyanogen bromide Hofmann elimination Alkene Proceeds by β-elimination of less hindered ... Such reactions, which are most useful for alkyl iodides and bromides, are rarely employed because the degree of alkylation is ...
Cusumano CL, Taniuchi H, Anfinsen CB (1968). "Staphylococcal nuclease (Foggi strain). I. Order of cyanogen bromide fragments ...
For example, cyanogen bromide cleaves the peptide bond after a methionine. Similar methods may be used to specifically cleave ...
Examples of cleaving agents used are cyanogen bromide, pepsin, and trypsin. Muller, P. (1 January 1994). "Glossary of terms ...
Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain". The Journal of Biological ...
Amino acid sequence of heavy-chain cyanogen bromide fragments H1-H4". Biochemistry. 9 (16): 3161-70. doi:10.1021/bi00818a008. ... 8. Amino acid sequence of heavy-chain cyanogen bromide fragments H5-H7". Biochemistry. 9 (16): 3171-81. doi:10.1021/bi00818a009 ... the cyanogenbromide cleavage products, and the disulfide bridges (author's transl)]". Hoppe-Seyler's Z. Physiol. Chem. 357 (11 ...
Xiao S, Pollock HG, Taurog A, Rawitch AB (1995). "Characterization of hormonogenic sites in an N-terminal, cyanogen bromide ...
The racemic synthesis involves addition/cyclization reaction of 2-amino-1-phenylethanol with cyanogen bromide. A similar ...
Treatment of that with cyanogen bromide under von Braun reaction conditions leads to the isolable aminocyanide. This is the ...
Smith M, Ratledge C, Crook S (1990). "Properties of cyanogen bromide-activated, Agarose-immobilized catechol 1,2-dioxygenase ...
Digestion is done either by endopeptidases such as trypsin or pepsin or by chemical reagents such as cyanogen bromide. ...
Green PR, Vanaman TC, Modrich P, Bell RM (1983). "Partial NH2- and COOH-terminal sequence and cyanogen bromide peptide analysis ...
Lux SE, John KM, Ronan R, Brewer HB (Dec 1972). "Isolation and characterization of the tryptic and cyanogen bromide peptides of ...
... , or its lactone form, is the product of a cyanogen bromide cleavage of a peptide by degradation of methionine. ...
Seyer JM, Kang AH (1989). "Covalent structure of collagen: amino acid sequence of three cyanogen bromide-derived peptides from ...
The cyanogen bromide, by comparison, transformed norephedrine into the cis isomer and norpseudoephedrine into the trans isomers ... The cyanate reaction proceeds differently from the cyanogen bromide and transforms norephedrine into trans-4-methylaminorex ... such as replacing cyanogen bromide with sodium or potassium cyanate to form an intermediate and then reacting it with ... generally synthesized from dl-phenylpropanolamine in one step by cyclization with cyanogen bromide (sometimes prepared in situ ...
Homoserine lactone is also a product of the proteolytic reaction of cyanogen bromide (CNBR) with a methionine residue in a ...
The use of cyanogen bromide for pyridine activation was independently reported by W. König: The synthesis and utility of Zincke ... A variation of the Zincke reaction has been applied in the synthesis of novel indoles: with cyanogen bromide mediated pyridine ...
Cacodyl Cyanogen bromide Dimethyl(trifluoromethylthio)arsine Diphenylcyanoarsine Mercury(II) cyanide Mercury oxycyanide ...
Common activation chemistries include cyanogen bromide (CNBr) activation and reductive amination of aldehydes to attach ...
Reduction of the nitro group leads to the aniline and reaction of this with cyanogen bromide possibly gives cyanamide 3 as the ...
... such as cyanogen bromide (BrCN), bromine thiocyanate (BrSCN), and bromine azide (BrN3). The pale-brown bromine monofluoride ( ... The bromide anion is not very toxic: a normal daily intake is 2 to 8 milligrams. However, high levels of bromide chronically ... Large amounts of bromide salts are toxic from the action of soluble bromide ions, causing bromism. However, a clear biological ... Potassium bromide and sodium bromide were used as anticonvulsants and sedatives in the late 19th and early 20th centuries, but ...
1972). "Isolation and partial characterization of the cyanogen bromide fragments of 1 -acid glycoprotein and the elucidation of ... the amino acid sequence of the carboxyl-terminal cyanogen bromide fragment". Biochemistry. 11 (20): 3817-29. doi:10.1021/ ...
Edelman and his colleagues used cyanogen bromide and proteases to fragment the antibody protein subunits into smaller pieces ...
"Cyanogen Bromide" (PDF). Organic Syntheses. 11: 30.. ; Collective Volume, 2, p. 150. ... Wikimedia Commons has media related to cyanogen.. Wikisource has the text of the 1911 Encyclopædia Britannica article Cyanogen. ... Cyanogen is the anhydride of oxamide: H2NC(O)C(O)NH2 → NCCN + 2 H2O. although oxamide is manufactured from cyanogen by ... Cyanogen is the chemical compound with the formula (CN)2. It is a colorless, toxic gas with a pungent odor. The molecule is a ...
By cleavage (tertiary amines only) with cyanogen bromide Hofmann elimination Alkene Proceeds by β-elimination of less hindered ... Such reactions, which are most useful for alkyl iodides and bromides, are rarely employed because the degree of alkylation is ...
The active ingredient in pepper spray is capsaicin, which is a chemical derived from the fruit of plants in the genus Capsicum, including chilis. Extraction of oleoresin capsicum (OC) from peppers requires capsicum to be finely ground, from which capsaicin is then extracted using an organic solvent such as ethanol. The solvent is then evaporated, and the remaining waxlike resin is the oleoresin capsaicin. An emulsifier such as propylene glycol is used to suspend OC in water, and pressurized to make it aerosol in pepper spray. High performance liquid chromatography (HPLC) is used to measure the amount of capsaicin and major capsaicinoids within pepper sprays. Determining the strength of different manufacturers of pepper sprays can be confusing and difficult. Statements a company makes about their product strength are not regulated. A method using the capsaicin and related capsaicinoids (CRC) content of the product is unreliable as well, because there are six different types of capsaicinoids, ...
During the Second World War cyanogen chloride's symbol was changed from CK to CC, but when it became apparent that CC marked ... Cyanogen. *Cyanogen bromide. *Cyanogen chloride (CK). *Hydrogen cyanide (AC). *Arsine. *Vinyl arsine ...
Lux SE, John KM, Ronan R, Brewer HB (Dec 1972). "Isolation and characterization of the tryptic and cyanogen bromide peptides of ...
... and ethyl bromide.[13] ... Bromide compounds (e.g., lithium bromide, potassium bromide, ...
Cyanogen. *Cyanogen bromide. *Cyanogen chloride (CK). *Hydrogen cyanide (AC). *Arsine. *Vinyl arsine ...
Examples of cleaving agents used are cyanogen bromide, pepsin, and trypsin.[6] ...
Bromide compounds (e.g., lithium bromide, potassium bromide, sodium bromide). *Carbamazepine. *Chloralose ...
Hartman, W. W.; Dreger, E. E. (1931). "Cyanogen Bromide". Org. Synth. 11: 30; Coll. Vol. 2: 150.. ...
Cyanogen. *Cyanogen bromide. *Cyanogen chloride (CK). *Hydrogen cyanide (AC). *Arsine. *Vinyl arsine ...
2, and Cl2F+.[42] Some pseudohalides of chlorine are also known, such as cyanogen chloride (ClCN, linear), chlorine cyanate ( ... Conversely, the chloride ion is a weaker reducing agent than bromide, but a stronger one than fluoride.[29] It is intermediate ...
More recently, it has become much more commonplace to use ethyl chloroformate instead of cyanogen bromide for the Von Braun ...
Click E.M., Bornstein P. (1970). Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 ...
Potassium bromide. Potassium iodide Other cations. Lithium chloride. Sodium chloride. Rubidium chloride. Caesium chloride. ...
Cyanogen. *Cyanogen bromide. *Cyanogen chloride (CK). *Hydrogen cyanide (AC). *Arsine. *Vinyl arsine ...
Xylyl bromide. Vomiting agents[edit]. These sensory irritants are also termed sternators or nose irritants. They irritate the ... Cyanogen chloride (CK). *Hydrogen cyanide (AC). *Arsine (SA). Choking agents[edit]. Main article: Pulmonary agent ...
Apart from these, some pseudohalides are also known, such as cyanogen bromide (BrCN), bromine thiocyanate (BrSCN), and bromine ... Hydrogen bromideEdit. The simplest compound of bromine is hydrogen bromide, HBr. It is mainly used in the production of ... Potassium bromide and sodium bromide were used as anticonvulsants and sedatives in the late 19th and early 20th centuries, but ... The bromide anion is not very toxic: a normal daily intake is 2 to 8 milligrams.[57] However, high levels of bromide ...
2 will react violently. High-concentration hydrogen peroxide streams, typically above 40%, should be considered hazardous due to concentrated hydrogen peroxide's meeting the definition of a DOT oxidizer according to U.S. regulations, if released into the environment. The EPA Reportable Quantity (RQ) for D001 hazardous wastes is 100 pounds (45 kg), or approximately 10 US gallons (38 L), of concentrated hydrogen peroxide. Hydrogen peroxide should be stored in a cool, dry, well-ventilated area and away from any flammable or combustible substances. It should be stored in a container composed of non-reactive materials such as stainless steel or glass (other materials including some plastics and aluminium alloys may also be suitable).[88] Because it breaks down quickly when exposed to light, it should be stored in an opaque container, and pharmaceutical formulations typically come in brown bottles that block light.[89] Hydrogen peroxide, either in pure or diluted form, can pose several risks, the main ...
Bromide in source waters can be converted by ozone into bromate, a potent carcinogen that is regulated in the United States, as ... cyanogen chloride, dibromoacetonitrile, dibromochloromethane, dichloroacetic acid, dichloroacetonitrile, NDMA, and ... as well as iodide and bromide ions, to produce a range of DBPs such as the trihalomethanes (THMs), haloacetic acids (HAAs), ... the concentration of natural organic matter and bromide/iodide, the time since dosing (i.e. water age), temperature, and pH of ...
5Na with trimethylammonium bromide.[4] The ion is bent too, with a H-C-H angle of about 103°.[8] ...
... to methyl bromide and phosphine. In some cases, however, residues on the grain result in flavours that are unacceptable to ...
Cyanogen iodide. *Cyanogen bromide. *Cyanogen chloride. *Cyanogen fluoride. *Acetonitrile. *Aminoacetonitrile. *Glycolonitrile ...
Xiao S, Pollock HG, Taurog A, Rawitch AB (1995). "Characterization of hormonogenic sites in an N-terminal, cyanogen bromide ...
Examples include cyanogen ((CN)2), triphosphorus pentanitride (P3N5), disulfur dinitride (S2N2), and tetrasulfur tetranitride ( ... Nitrosyl bromide (NOBr) is red. The reactions of the nitryl halides are mostly similar: nitryl fluoride (FNO2) and nitryl ...
Examples include cyanogen ((CN)2), triphosphorus pentanitride (P3N5), disulfur dinitride (S2N2), and tetrasulfur tetranitride ( ... Nitrosyl bromide (NOBr) is red. The reactions of the nitryl halides are mostly similar: nitryl fluoride (FNO2) and nitryl ...
Cyanogen bromide can be stored under dry conditions at 2 to 8 °C for extended periods. Cyanogen bromide is volatile, and ... "Cyanogen Bromide HSDB 708". HSDB. NIH / NLM. 2009-04-07. Lunn, G.; Sansone, E. B. (1985). "Destruction of Cyanogen Bromide and ... "Cyanogen Bromide MSDS Number: C6600". J. T. Baker. 1996-08-12. Teeri, A. E. (1948). "Thiamine and the Cyanogen Bromide Reaction ... Like some other cyanogen compounds, cyanogen bromide undergoes an exothermic trimerisation to cyanuric bromide ((BrCN)3). This ...
Bromure de cyanogen; Cyanogen bromide (BrCN); TL 822; Cyanogen bromide ((CN)Br); Rcra waste number U246; UN 1889; Bromine ... Baxter, G.P.; Bezzenberger, F.K.; Wilson, C.H., THE VAPOR PRESSURES OF CERTAIN SUBSTANCES: CHLORO-PICRIN, CYANOGEN BROMIDE, ... Lord, G.; Woolf, A.A., The cyanogen halides. Part III. Their heats of formation and free energies, J. Chem. Soc., 1954, 2546. [ ... Lord, G.; Woolf, A.A., The cyanogen halides. Part III. Their heats of formation and free energies, J. Chem. Soc., 1954, 2546- ...
Bromure de cyanogen; Cyanogen bromide (BrCN); TL 822; Cyanogen bromide ((CN)Br); Rcra waste number U246; UN 1889; Bromine ... Lord, G.; Woolf, A.A., The cyanogen halides. Part III. Their heats of formation and free energies, J. Chem. Soc., 1954, 2546- ... Other names: Bromine cyanide; Bromocyan; Bromocyanide; Bromocyanogen; Campilit; Cyanobromide; Cyanogen monobromide; BrCN; (CN) ...
... D.M. Bunk dmb618 at enh.nist.gov Fri Mar 31 10:20:32 EST 1995 *Previous message: Tropix vs. ... I am planning on doing a cyanogen bromide digest of huamn serum albumin next week and I was looking for some pointers from ...
... Joe Mack mack at ncifcrf.gov Fri Jan 28 13:20:36 EST 1994 * ...
We also Provide Trading Suppliers & Manufacture for 506-68-3 Cyanogen bromide. ... Cyanogen bromide is slightly soluble in water. Cyanogen bromide is gradually decomposed by water and very rapidly by acids to ... Cyanogen bromide is slightly soluble in water. Cyanogen bromide is gradually decomposed by water and very rapidly by acids to ... Cyanogen bromide is not combustible itself, but impure Cyanogen bromide decomposes rapidly and tends to explode. A violent ...
Disease relevance of CYANOGEN BROMIDE. *Radiolabel sequence analysis of cyanogen bromide fragments of p42 led to the conclusion ... Biological context of CYANOGEN BROMIDE. *Amino acid and cyanogen bromide fragmentation studies showed a close similarity ... Gene context of CYANOGEN BROMIDE. *However, the COOH-terminal cyanogen bromide fragment corresponding to residues 60--78 ... Sequences of the cyanogen bromide peptides from the alpha chain. Huynh, Q.K., Vaaler, G.L., Recsei, P.A., Snell, E.E. J. Biol. ...
Cyanogen Bromide Electrophoresis, Polyacrylamide Gel English Abstract Insect Viruses - analysis Peptides Sodium Dodecyl Sulfate ... The cyanogen bromide cleavage of acetic polyhedral protein from nuclear polyhedrosis virus of B. mori was performed. Two ... Isolation and characteristics of fragments from the cyanogen bromide splitting of inclusion body proteins of Bombyx mori ... which consist of 29 and 34 amino acid residue were isolated from a mixture of cyanogen bromide fragments. The amino acid ...
Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments. G J Arlaud, J Gagnon, R R ... Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments ... Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments ... Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments ...
Bromine cyanide; Bromine monocyanide; Bromocyanide; Bromocyanogen; Campilit; Cyanic bromide; Cyanobromide; Cyanogen bromide; ...
Cyanogen bromide cation. [BrCN]+ (g). 1331.3. 1325.0. ± 1.1. kJ/mol. 105.9209 ±. 0.0013. 34749-77-4*0. ... Cyanogen bromide anion. [BrCN]- (g). 57.9. 54.2. ± 3.8. kJ/mol. 105.9220 ±. 0.0013. 54092-05-6*0. ... Cyanogen bromide. BrCN (g). 186.7. 180.2. ± 1.1. kJ/mol. 105.9214 ±. 0.0013. 506-68-3*0. ... Isocyanogen bromide anion. [BrNC]- (g). 105.0. 101.8. ± 4.6. kJ/mol. 105.9220 ±. 0.0013. *238754-53-5*0. ...
Manufacturer Supplier of CYANOGEN BROMIDE based in Mumbai, India ... CETYL TRIMETHYL AMMONIUM BROMIDE. *N-CETYL-N,N,N, TRIMETHYL ...
Alfa-amylase showed optimal activity at pH 6.0 Cyanogen bromide was prepared and was used to activate sephadex G200 at pH 11.5 ... The volume of the cyanogen bromide activated gel, at this pH decreased by about 50 percent, compared to that of the unactivated ... Alfa-amylase was coupled to cyanogen bromide activated Sephadex G200 at pH8.3 and 7.0. Coupling of the enzyme led to further ... ATTYGALLE, AB, Studies on immobilization of alfa- amylase to cyanogen bromide activated sephadex g 200, University of Sri Lanka ...
Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen. ... Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen. Authors : Kang A H , ... 4313735] Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen.. ...
Preparation of GNA Covalently Coupled to Agarose using Cyanogen Bromide. Cyanogen bromide (CNBr) activated agarose was used for ... Said means include avidin-streptavidin, cynanogen bromide coupling, the use of a linker such as a polyethylene glycol linker. A ...
506-68-3.................................. Cyanogen bromide*. 506-78-5.................................. Cyanogen iodide. 506- ...
Cyanogen bromide - CNBr. *Cyanogen chloride - CNCl. *Cyanogen iodide - ICN. *Cyanogen - (CN)2 ...
NMR on single crystals of potassium cyanogen bromide (a measurement of the orientational probability distribution function of ... Walton, Jeffrey Howard, "NMR on single crystals of potassium cyanogen bromide (a measurement of the orientational probability ... distribution function of the negatively charged cyanogen ion)" (1989). Dissertations, Theses, and Masters Projects. Paper ...
Cyanogen Bromide CAS RN:506-68-3. Key Info. SUBSTANCES - TOXIC and/or CORROSIVE (Non-Combustible/Water-Sensitive). • TOXIC; ...
Cyanogen Bromide. 1,000. 500/10,000 506-78-5. Cyanogen Iodide. 1,000. 1,000/10,000 ...
His studies with bromine led to the preparation of ethyl bromide; cyanogen bromide; a selenium bromide; several compounds of ... In 1824 he prepared cyanogen iodide (discovered by Humphry Davy in 1816) by a more efficient method. ...
Glass bottle packed in tin can Cyanogen bromide, 97%, ACROS Organics™ Cyanofluor to Cyclob -Organics ...
Cyanogen chloride and cyanogen bromide each trimerize at elevated temperatures over a carbon catalyst. The chloride gives ... Morris, Joel; Kovács, Lajos; Ohe, Kouichi (2015). "Cyanogen Bromide". Encyclopedia of Reagents for Organic Synthesis. pp. 1-8. ... Joel Morris; Lajos Kovács (2008). "Cyanogen Bromide". Encyclopedia of Reagents for Organic Synthesis. doi:10.1002/047084289X. ... Like the chloride, it undergoes ab exothermic trimerisation to form cyanuric bromide. This reaction is catalyzed by traces of ...
Coupling of Proteins to Cyanogen Bromide-activated Sepharose 4B.. The CVF, anti-C1-INH, and anti-HSA were coupled to CNBr- ...
Cyanogen bromide. Diethyl sulfide. Hydrocyanic acid. Iodine pentafluoride. Kendalite. Magnesium arsenide. Martonite. ... Cyanogen chloride. Diisopropyl methylphosphonate. Dimethyldisulfide. Dimethyl methylphosphonate. Diphenylchlorarsine. ...
The preparation of Cyanogen Bromide is covered in another document of mine. This compound should only be prepared in an area of ... 1.1 Moles Cyanogen Bromide (MW: 105.93) *3.0 Moles of Sodium Acetate (MW: 82.04) The Sodium Acetate may be prepared by ... Add the Cyanogen Bromide solution to the flask though the addition funnel over a period of 15 minutes with stirring. * React ... Cyanogen Bromide acts on cytochrome oxidase just like any other cyanide and can kill you quite effectively and quickly. Also, ...
... are also susceptible to cyanogen bromide cleavage.. AB - Characterization of the cyanogen bromide (CNBr) fragments of the β ... Characterization of the cyanogen bromide fragments of the β chain of human haptoglobin. / Kurosky, Alexander; Hay, Regine E.; ... Characterization of the cyanogen bromide fragments of the β chain of human haptoglobin. Biochemistry. 1976;15(24):5326-5336. ... Cyanogen bromide reaction of intact haptoglobin 1-1 resulted in the isolation of a β-chain fragment, CNBr III, covalently ...
Cyanides and Cyanogen Bromide 129. Cylindrospermopsin 137. Diisopropyl Fluorophosphate 141. Dimethyl Sulfate and Related ...
Schwartz, P. L., & McHugh, N. J. (1978). Tests for cataglykin activity on a cyanogen bromide fragment of human growth hormone. ... Tests for cataglykin activity on a cyanogen bromide fragment of human growth hormone. / Schwartz, P L; McHugh, N J. ... Schwartz, PL & McHugh, NJ 1978, Tests for cataglykin activity on a cyanogen bromide fragment of human growth hormone, ... Tests for cataglykin activity on a cyanogen bromide fragment of human growth hormone. In: Metabolism. 1978 ; Vol. 27, No. 1. pp ...
  • The cyanogen bromide cleavage of 'acetic' polyhedral protein from nuclear polyhedrosis virus of B. mori was performed. (arctichealth.org)
  • Characterization of the cyanogen bromide (CNBr) fragments of the β chain of human haptoglobin revealed five major fragments resulting from cleavage of four methionyl residues. (utmb.edu)
  • These minor cleavage products give evidence that tryptophanyl residues in proteins, or glycoproteins, are also susceptible to cyanogen bromide cleavage. (utmb.edu)
  • A peptide having the reputed essential amino acid sequence to show cataglykin-like effects was prepared from human growth hormone (hGH) by cyanogen bromide cleavage and was tested in two systems in which cataglykin has effects. (bath.ac.uk)
  • Analysis of high molecular mass proteins larger than 150 kDa using cyanogen bromide cleavage and conventional 2-DE. (cngb.org)
  • Cleavage of peptide bond by cyanogen bromide 2 ii. (scribd.com)
  • Four methionine substitutions and two alanine substitutions were introduced at fixed positions in Sup(1-61) to allow cyanogen bromide cleavage to facilitate subsequent mass spectrometry analysis. (pubmedcentralcanada.ca)
  • Cleavage of a fusion protein with cyanogen bromide. (wikipathways.org)
  • Two peptides BrCN-II and BrCN-II' which consist of 29 and 34 amino acid residue were isolated from a mixture of cyanogen bromide fragments. (arctichealth.org)
  • Compositional analyses of the five cyanogen bromide fragments accounted for 248-253 amino acid residues in agreement with the number of residues determined for the intact β chain. (utmb.edu)
  • Automated amino-terminal sequence analysis and carboxyl-terminal hydrolysis with carboxypeptidase of the haptoglobin β chain and cyanogen bromide fragments identified 139 residues, or about 55% of the β-chain molecule. (utmb.edu)
  • Microsequencing of peptide fragments from a cyanogen bromide digest of p78 identified this protein as BiP and sequence analysis identified p74 as the peptidyl-prolyl cis-trans isomerase, FKPB65. (rupress.org)
  • I am planning on doing a cyanogen bromide digest of huamn serum albumin next week and I was looking for some pointers from anyone with CNBr digest experience. (bio.net)
  • Cyanogen bromide reaction of intact haptoglobin 1-1 resulted in the isolation of a β-chain fragment, CNBr III, covalently attached to the intact α 1 chain by a single disulfide bond. (utmb.edu)
  • Cyanogen chloride (CK) is a highly volatile and toxic chemical asphyxiant that interferes with the body's ability to use oxygen. (cdc.gov)
  • Exposure to cyanogen chloride (CK) can be rapidly fatal. (cdc.gov)
  • Cyanogen chloride (CK) has strong irritant and choking effects. (cdc.gov)
  • Cyanogen chloride (CK) is a chemical warfare agent (military designation CK). (cdc.gov)
  • Indoor Air: Cyanogen chloride (CK) can be released into indoor air as a liquid spray (aerosol) or as a gas. (cdc.gov)
  • Water: Cyanogen chloride (CK) can be used to contaminate water. (cdc.gov)
  • Agricultural: If cyanogen chloride (CK) is released into the air as a liquid spray (aerosol), it has the potential to contaminate agricultural products. (cdc.gov)
  • If cyanogen chloride (CK) is released as a gas, it is highly unlikely to contaminate agricultural products. (cdc.gov)
  • Cyanogen chloride (CK) can affect the body by inhalation, ingestion, skin contact, or eye contact. (cdc.gov)
  • Cyanogens may be simple (cyanogen chloride) or complex (sodium nitroprusside). (fas.org)
  • AC ) and the simple cyanogen, cyanogen chloride ( CK ). (fas.org)
  • This process was commercialized: Symmetrical 1,3,5-triazines are prepared by trimerization of certain nitriles such as cyanogen chloride or cyanimide. (wikipedia.org)
  • Cyanogen chloride and cyanogen bromide each trimerize at elevated temperatures over a carbon catalyst. (wikipedia.org)
  • The chloride gives cyanuric chloride: The bromide has an extended shelflife when refrigerated. (wikipedia.org)
  • Like the chloride, it undergoes ab exothermic trimerisation to form cyanuric bromide. (wikipedia.org)
  • Cyanogen bromide is the inorganic compound with the formula (CN)Br or BrCN. (wikipedia.org)
  • Like some other cyanogen compounds, cyanogen bromide undergoes an exothermic trimerisation to cyanuric bromide ((BrCN)3). (wikipedia.org)
  • Gentaur antibody-antibodies.com The Marketplace for Antibodies : Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen. (antibody-antibodies.com)
  • 125I-labeled HGF was incubated with collagens I-VI, single collagen chains and their cyanogen bromide peptides, with fibronectin, fibrinogen, and laminin that were either immobilized on polystyrene or blotted to nitrocellulose after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. (nih.gov)
  • Fragmentation with cyanogen bromide indicated unique collagenous peptides mediating the interaction. (nih.gov)
  • Tryptic peptides and cyanogen bromide peptides of native bovine S antigen were purified and partially sequenced. (pnas.org)
  • The carbon atom in cyanogen bromide is bonded to bromine by a single bond and to nitrogen by a triple bond (i.e. (wikipedia.org)
  • Cyanogen bromide can be prepared by oxidation of sodium cyanide with bromine, which proceeds in two steps via the intermediate cyanogen ((CN)2): 2 NaCN + Br2 → (CN)2 + 2 NaBr (CN)2 + Br2 → 2 (CN)Br When refrigerated the material has an extended shelflife. (wikipedia.org)
  • The electron density in cyanogen bromide is shifted away from the carbon atom, making it unusually electrophilic, and towards the more electronegative bromine and nitrogen. (wikipedia.org)
  • When material is heated to decomposition, Cyanogen bromide emits very toxic fumes of cyanide and bromide. (lookchem.com)
  • Cyanogen bromide is hydrolyzed to release hydrogen cyanide and hypobromous acid (CN)Br + H2O → HCN + HOBr The main uses of cyanogen bromide are to immobilize proteins, fragment proteins by cleaving peptide bonds, and synthesize cyanamides and other molecules. (wikipedia.org)
  • If the sulfur in cysteine attacked cyanogen bromide, the bromide ion would deprotonate the cyanide adduct, leaving the sulfur uncharged and the beta carbon of the cysteine not electrophilic. (wikipedia.org)
  • Cyanogen is typically generated from cyanide compounds. (wikipedia.org)
  • Alternatively, one can combine solutions of copper(II) salts (such as copper(II) sulfate ) with cyanides, an unstable copper(II) cyanide is formed which rapidly decomposes into copper(I) cyanide and cyanogen. (wikipedia.org)
  • It can also be prepared by heating silver cyanide , silver cyanate , cyanogen iodide or cyanuric iodide. (wikipedia.org)
  • A cyanogen usually refers to a nitrile that liberates the cyanide anion during metabolism and produces the biological effects of the cyanide anion. (fas.org)
  • The fruits and seeds (especially pits) of many plants, such as cherries, peaches, almonds, and lima beans, contain cyanogens capable of releasing free cyanide following enzymatic degradation. (fas.org)
  • Recycling Cyanogen bromide activated sepharose affinity columns? (bio.net)
  • The affinity method of isolating lactoferrin is based on the use of a specific immunosorbent consisting of antibodies to lactoferrin covalently conjugated with cyanogen-bromide-activated Sepharose 4B. (springer.com)
  • In 1824 he prepared cyanogen iodide (discovered by Humphry Davy in 1816) by a more efficient method. (encyclopedia.com)
  • Cyanogen bromide is often used to immobilize proteins by coupling them to reagents such as agarose for affinity chromatography. (wikipedia.org)
  • Cyanogen bromide is also often used because it reacts with the hydroxyl groups on agarose to form cyanate esters and imidocarbonates. (wikipedia.org)
  • Also, cyanogen bromide activation involves the attachment of a ligand to agarose by an isourea bond, which is positively charged at neutral pH and thus unstable. (wikipedia.org)
  • Antibodies were coupled to agarose beads using a cyanogen bromide method. (abcam.com)
  • A simplified method for cyanogen bromide activation of agarose for affinity chromatography. (alfa.com)
  • [6] The name is also used for the CN radical, [7] and hence is used for compounds such as cyanogen bromide (NCBr). (wikipedia.org)
  • Subfragment-1 was prepared from adult chicken gizzard myosin by limited digestion with papain, and a 137-residue peptide was obtained by cleaving subfragment-1 with cyanogen bromide. (nagasaki-u.ac.jp)
  • The cyanogen halides. (nist.gov)
  • Benzene and cyanogen halides yield HCl as a byproduct (Hagedorn, F. H. Gelbke, and Federal Republic of Germany. (lookchem.com)
  • Cyanogen bromide is not combustible itself, but impure Cyanogen bromide decomposes rapidly and tends to explode. (lookchem.com)
  • C98105 Reaction of Imidazoles with Cyanogen Bromide: Cyanation at N 1 or Bromination at C 2? (publish.csiro.au)
  • Cyanogen molecules consist of two CN groups - analogous to diatomic halogen molecules, such as Cl 2 , but far less oxidizing. (wikipedia.org)
  • Cyanogen is the chemical compound with the formula ( C N ) 2 . (wikipedia.org)
  • Clothing for fire-fighters (including helmets, protective boots and gloves) conforming to European standard EN 469 will provide a basic level of protection for chemical incidents. (europa.eu)
  • The disadvantages of this approach include the toxicity of cyanogen bromide and its sensitivity to oxidation. (wikipedia.org)
  • Because of its simplicity and mild pH conditions, cyanogen bromide activation is the most common method for preparing affinity gels. (wikipedia.org)
  • Cyanogen was first synthesized in 1815 by Joseph Louis Gay-Lussac , who determined its empirical formula and named it. (wikipedia.org)
  • Furthermore, after cleaving the specific [ 125 I]IAF-photolabeled σ-1 receptor in guinea pig and rat liver membranes and the pure guinea pig σ-1 receptor with EndoLys-C and cyanogen bromide, the [ 125 I]IAF label was identified both in a peptide containing steroid binding domain-like I (SBDLI) (amino acids 91-109) and in a peptide containing steroid binding domain-like II (SBDLII) (amino acids 176-194). (aspetjournals.org)
  • Paracyanogen can also be converted back to cyanogen by heating to 800 °C (1,470 °F). [9] Based on experimental evidence, the structure of this polymeric material is thought to be rather irregular, with most of the carbon atoms being of sp 2 type and localized domains of π conjugation. (wikipedia.org)
  • Cyanogen Bromide (Bromocyanogen), C N Br , resembles Cyanogen Chloride, CNCl in its manner of preparation, being formed by the action of bromine on hydrocyanic acid or a cyanide. (atomistry.com)
  • The pseudohalogens, a collection of species which includes cyanogen chloride, cyanogen bromide, and iodine azide. (chemthes.com)
  • Thioanion displaces chloride from cyanogen chloride, forming the thiocyanate, yet thiol displaces cyanide ion from cyanogen bromide. (chemthes.com)
  • 1993. A rapid and simple analytical method for cyanogen chloride and cyanogen bromide in drinking water . (umass.edu)
  • Sodium Cyanide found uses in gold mining, to produce cyanuric chloride, cyanogen chloride and to prepare nitriles. (worldofchemicals.com)
  • It is widely used for the preparation of other bromides in organic synthesis and other areas. (worldofchemicals.com)
  • Two new polypseudohalogen compounds derived from cyanogen bromide have the unusual property that they can dissolve gold at room temperature. (dewdropsystems.in)
  • It is a strong oxidant, mainly used in continuous or batch dyeing processes involving sulfur or vat dyes and as a hair-permagent, chemical agent, or gold solvent in gold mines when used with sodium bromide. (worldofchemicals.com)