Cyanogen Bromide: 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.Bromides: 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)Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Amino Acid Sequence: 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.Trypsin: 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.Amino Acids: 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.Chymotrypsin: 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.Thermolysin: A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.Pepsin A: 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.Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Molecular Weight: The sum of the weight of all the atoms in a molecule.Molecular Sequence Data: 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.Peptide Mapping: 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, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.Collagen: 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).Ethidium: 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.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Macromolecular Substances: 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.Cattle: 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.Peptides: 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.Chromatography, Ion Exchange: 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.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Rabbits: 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.Phosphoglycerate Kinase: 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.Affinity Labels: 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.Protein Conformation: 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).Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Lathyrism: 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.Hydrocarbons, BrominatedPhotoaffinity Labels: 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.Procollagen: A biosynthetic precursor of collagen containing additional amino acid sequences at the amino-terminal and carboxyl-terminal ends of the polypeptide chains.Leucyl Aminopeptidase: 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.Ipratropium: 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.Dansyl Compounds: Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group.Escherichia coli: 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.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Galactosidases: A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.Epitopes: Sites on an antigen that interact with specific antibodies.MaleatesHydroxylysine: A hydroxylated derivative of the amino acid LYSINE that is present in certain collagens.Chromatography, Affinity: 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)Iodobenzoates: Benzoic acid esters or salts substituted with one or more iodine atoms.Hydroxylamine: A colorless inorganic compound (HONH2) used in organic synthesis and as a reducing agent, due to its ability to donate nitric oxide.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Carbohydrates: 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.Species Specificity: 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.Muscles: Contractile tissue that produces movement in animals.Kinetics: The rate dynamics in chemical or physical systems.MNSs Blood-Group System: 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.Cyanides: 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.Hydroxylamines: Organic compounds that contain the (-NH2OH) radical.Papain: 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.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Chromatography: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Electrophoresis: 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.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Bromosuccinimide: 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,).Atropine Derivatives: Analogs and derivatives of atropine.Osteogenesis Imperfecta: 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.Butylscopolammonium Bromide: 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.Sequence Homology, Nucleic Acid: 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.Immunodiffusion: Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.Crotalid Venoms: 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.CarbodiimidesProtein Binding: 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.Chromatography, Paper: 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).Horses: 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.Carboxypeptidase B: 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.Cystine: 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.Neurospora: 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)Cloning, Molecular: 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.Chromatography, Agarose: 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.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Troponin: 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.Structure-Activity Relationship: 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.Lysine: An essential amino acid. It is often added to animal feed.Swine: 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).Chickens: 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 ...
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.
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 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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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.
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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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. ...
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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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1. The a- and b-chains of reduced and alkylated human complement subcomponent C1r were separated by high-pressure gel-permeation chromatography and isolated in good yield and in pure form. 2. CNBr cleavage of C1r b-chain yielded eight major peptides, which were purified by gel filtration and high-pressure reversed-phase chromatography. As determined from the sum of their amino acid compositions, these peptides accounted for a minimum molecular weight of 28 000, close to the value 29 100 calculated from the whole b-chain. 3. N-Terminal sequence determinations of C1r b-chain and its CNBr-cleavage peptides allowed the identification of about two-thirds of the amino acids of C1r b-chain. From our results, and on the basis of homology with other serine proteinases, an alignment of the eight CNBr-cleavage peptides from C1r b-chain is proposed. 4. The residues forming the charge-relay system of the active site of serine proteinases (His-57, Asp-102 and Ser-195 in the chymotrypsinogen numbering) are ...
Recent biochemical studies of p190, a calmodulin (CM)-binding protein purified from vertebrate brain, have demonstrated that this protein, purified as a complex with bound CM, shares a number of properties with myosins (Espindola, F. S., E. M. Espreafico, M. V. Coelho, A. R. Martins, F. R. C. Costa, M. S. Mooseker, and R. E. Larson. 1992. J. Cell Biol. 118:359-368). To determine whether or not p190 was a member of the myosin family of proteins, a set of overlapping cDNAs encoding the full-length protein sequence of chicken brain p190 was isolated and sequenced. Verification that the deduced primary structure was that of p190 was demonstrated through microsequence analysis of a cyanogen bromide peptide generated from chick brain p190. The deduced primary structure of chicken brain p190 revealed that this 1,830-amino acid (aa) 212,509-D) protein is a member of a novel structural class of unconventional myosins that includes the gene products encoded by the dilute locus of mouse and the MYO2 gene ...
Several peptides were isolated from tryptic digests of insoluble calf aorta matrix by chromatography. Reductive pyridylethylation of a tryptic 15 kDa pool released fragments deriving from the C-terminus of type III collagen. A 50-residue peptide TC(III) was shown by sequence analysis to be the C-terminal peptide from the α1(III)-chain, containing a helical and non-helical region of equal sizes. The peptide was further digested with collagenase to give ColC(III), comprising the complete C-terminal non-helical region of α1(III) including a hydroxylysine in position 16C. The peptide TC(III)×TN(III) was isolated, demonstrating covalent cross-linking between the C-terminal non-helical region of one type III molecule and the N-terminal helical cross-linking region of another. Its digestion with cyanogen bromide yielded the small fragments α1(III)CB3B* and α1(III)CB3C, confirming TN(III) as an N-terminal helical cross-link site. Sequence analysis of both TC(III)×TN(III) and its ...
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standard methods and subjected to complete amino acid sequence analysis. An important part of these studies will be the selection of appropriate ...
Looking for Natural Bromides? Find out information about Natural Bromides. a group of rare minerals related to the halogen compounds. The minerals known in nature are limited to the silver bromides, which crystallize in a cubic... Explanation of Natural Bromides
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... - Free download as PDF File (.pdf), Text File (.txt) or read online for free. Amino acids are the building blocks of proteins. Many amino acids are produced by the body, however 8 must be obtainex
Potassium bromide is used in making bromide and iodo bromide photographic emulsions as well as in many developer formulas, where it performs the role of a restrainer. ​One packet contains 100 grams of potassium bromide, analytical grade.
potassium bromide chemical properties, What are the chemical properties of potassium bromide 7758-02-3, What are the physical properties of potassium bromide ect.
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102432-99-5 - OGOFNOBHYBYEBE-JQVQXGNYSA-M - 1-alpha-H,5-alpha-H-Tropanium, 3-hydroxy-8-(p-octylbenzyl)-, bromide, xanthene-9-carboxylate (ester) - Similar structures search, synonyms, formulas, resource links, and other chemical information.
The complete amino acid sequence of bovine S antigen (48-kDa protein) has been determined by cDNA and partial amino acid sequencing. A 1623-base-pair (bp) cDNA contains an open reading frame coding for a protein of 404 amino acids (45,275 Da). Tryptic peptides and cyanogen bromide peptides of native bovine S antigen were purified and partially sequenced. All of these peptides were accounted for in the long open reading frame. Searching of the National Biomedical Research Foundation data bank revealed no extensive sequence homology between S antigen and other proteins. However, there are local regions of sequence similarity with alpha transducin, including the sites subject to ADP-ribosylation by Bordetella pertussis and cholera toxins and the phosphoryl binding-sites. Secondary structure prediction and circular dichroic spectroscopy show that S antigen is composed predominantly of beta-sheet conformation. Acid-catalyzed methanolysis suggests the presence of low levels of carbohydrate in the ...
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Article A colorimetric microwell method for determining bromide concentrations. Bromide is commonly used as a tracer in studies of water and chemical transport in soil and rock because it is relatively nonreactive with soil and rock constituents and ...
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OBJECTIVES--To analyse the collagen composition of normal adult human supraspinatus tendon and to compare with: (1) a flexor tendon (the common biceps tendon) which is rarely involved in any degenerative pathology; (2) degenerate tendons from patients with chronic rotator cuff tendinitis. METHODS--Total collagen content, collagen solubility and collagen type were investigated by hydroxyproline analysis, acetic acid and pepsin digestion, cyanogen bromide peptide analysis, SDS-PAGE and Western blotting. RESULTS--The collagen content of the normal cadaver supraspinatus tendons (n = 60) was 96.3 micrograms HYPRO/mg dry weight (range 79.3-113.3) and there was no significant change across the age range 11 to 95 years. There was no significant difference from the common biceps tendon [93.3 (13.5) micrograms HYPRO/mg dry weight, n = 24]. Although extremely insoluble in both acetic acid and pepsin, much of the collagen was soluble after cyanogen bromide digestion [mean 47.9% (29.8)]. Seventeen per cent ...
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Sodium Bromide molecular formula:NaBr. molecular weight:102.9. CAS NO: 7647-15-6. Usage::This product is used for making sensitive emulsion of photographic film and for making medicinal intermediates in medico-industries, e.g. diuretic , sedative etc. It is also used as bromide making complex material and complex dyes.. Specifications:. ...
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Definition of primary structure - the characteristic sequence of amino acids forming a protein or polypeptide chain, considered as the most basic element of its str
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We report the molecular defect of albumin Herborn, a new genetic variant of human serum albumin which has been found in Germany. Isoelectric focusing analysis of CNBr fragments from the purified variant allowed us to localize the mutation in fragment CNBr 3 (residues 124-298). This fragment was isolated on a preparative scale and subjected to tryptic and V8 protease digestion. Sequence determination of the abnormal tryptic and V8 peptides revealed that the variant arises from the substitution Lys240→Glu. The -2 charge change of albumin Herborn, which is probably due to a A→G transition in the first position of the corresponding codon in the structural gene, has no significant effect on its electrophoretic mobility under non-denaturating conditions. Therefore we have assumed that residue 240, which has been implicated in the bilirubin primary binding site (Jacobsen, C. (1978) Biochem. J. 171, 453-459), is buried. The binding of bilirubin and biliverdin by albumin Herborn was quantified using ...
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Looking for bromide? Find out information about bromide. any of a group of compounds that contain bromine bromine , volatile, liquid chemical element; symbol Br; at. no. 35; at. wt. 79.904; m.p. -7.2°C;; b.p.... Explanation of bromide
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Serveral arguments that justify establishing a revised abundance calibration for DDO photometry of population I red giants are presented. The components of the blanketing vector in the DDO C(45-48) vs C(42-45) diagram are determined for late-type dwarfs and giants. We have redefined the DDO cyanogen anomaly and calibrated it against metallicity. The sample of field giants now available with abundances derived from high dispersion spectroscopy is substantially larger than previously available, leading to a more accurate abundance calibration. Iso-abundance lines in the C(41-42) vs C(42-45) diagram have been determined for population I G and K giants and an iterative method for deriving abundance of these stars is described. We show that the new DDO abundance are in very good agreement with those derived from high dispersion spectroscopy.The new method improves by about 0.1 dex the DDO abundances derived for early G and/or late K giants, with respect to the delta CN method of Janes (1975).. ...
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The present invention is related to a polypeptide solution which is obtained by dissolving, in a solvent including formic acid, or a solvent including an aprotic polar solvent having a dipole moment of 3.0 D or higher, and an inorganic s ...
I am growing MCF-7 cell line. I have been trying to stain dead cells using ethidium bromide and I havnt been very successful. I found the protocol online but it doesnt seem to work. if there is any other method with which I can stain the cells please let me know. Thanks in advance ...
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b) If you were told this piece of RNA carries the code for 5 amino acids, would you change your answer to part a? If so, what would your explanation be for change ...
The use of cyclic peptides in one-bead-one-compound libraries is limited by difficulties in sequencing hit compounds. Lacking a free N-terminal amine, such peptides cannot be sequenced by the Edman degradation approach, and complex fragmentation patterns are obtained by tandem mass spectrometry. To overcome this problem, we designed an alternative approach introducing a methionine residue within the macrocycle and as a linker to allow simultaneous ring-opening and release from the resin upon treatment with cyanogen bromide. The methionine linker was inverted relative to the peptide chain to allow the synthesis of cyclic peptides anchored by a lysine side chain and to avoid the presence of two C-terminal homoserine lactones on the released linear peptides. After MALDI-TOF MS/MS analysis, the peptides released from a single bead were sequenced manually and with a de novo sequencing software. The strategy described herein is compatible with commonly used amino acids and allows sequencing of cyclic ...
Samples of discs and disc attachments were extracted by dissociative methods and the resultant collagenous residues cleaved with cyanogen bromide. Soluble peptides thus released were characterized by their electrophoretic mobility following SDS-PAGE and by Western blot staining with specific antibodies against type I and type III collagens. Type III collagen was identified in samples taken from the posterior discal attachments. This may explain why this disc is prone to detachment and internal derangement and the high incidence of patients with temporomandibular joint dysfunction.
Cyanogen bromide - CNBr. *Cyanogen chloride - CNCl. *Cyanogen iodide - ICN. *Cyanogen - (CN)2 ...
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 ...
Cyanogen bromide cleavage and N-terminal sequences of the fragments". The Biochemical Journal. 215 (3): 565-71. doi:10.1042/ ...
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 ...
The von Braun reaction is an organic reaction in which a tertiary amine reacts with cyanogen bromide to an organocyanamide. An ... "The Von Braun Cyanogen Bromide Reaction". Organic Reactions. 7 (4): 198-262. doi:10.1002/0471264180.or007.04. Jie Jack Li (2014 ... the trimethylamine reacts with the cyanogen bromide to form a cyano group. This results in a quaternary ammonium salt, which in ...
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. ...
1-Naphthylamine is reacted with cyanogen bromide to give 2. Treatment of this intermediate with 3-ethyl-N-methylaniline leads ...
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 ...
Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain". J. Biol. Chem. 251: 1955-1959. ...
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 ...
Reduction of the nitro group leads to the aniline and reaction of this with cyanogen bromide possibly gives cyanamide 3 as 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 ...
Click E.M., Bornstein P. (1970). Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 ...
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 ...
"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 ...
More recently, it has become much more commonplace to use ethyl chloroformate instead of cyanogen bromide for the Von Braun ...
... 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 ...
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) ...
... Joe Mack mack at ncifcrf.gov Fri Jan 28 13:20:36 EST 1994 * ...
Cyanogen bromide can be cyclotrimerized to yield cyanuric bromide: 3 BrCN → (BrCN)3 Cyanogen bromide can be stored under dry ... "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 undergo an exothermic trimerisation to cyanuric bromide ((BrCN)3). This ...
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. ...
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 ...
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.. ...
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; ...
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 ...
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. ...
... 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 ...
Cyanogen Bromide. LinkOut - more resources. Other Literature Sources. *Cited by Patents in - The Lens ...
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 amino acid sequence of a cyanogen bromide-generated peptide corresponding to the region of subfragment-1 of chicken gizzard ... Direct Sequence Analysis of a Cyanogen Bromide-Generated Peptide Corresponding to the Region of Subfragment-1 of Adult Chicken ... Direct Sequence Analysis of a Cyanogen Bromide-Generated Peptide Corresponding to the Region of Subfragment-1 of Adult Chicken ... and a 137-residue peptide was obtained by cleaving subfragment-1 with cyanogen bromide. Amino acid composition analysis and ...
CYANOGEN BROMIDE (NEW TLV). LITHIUM HYDRIDE. METHYL FORMATE. OXALIC ACID, ANHYDROUS and DIHYDRATE. 1,2,3-TRICHLOROPROPANE. ... ALLY BROMIDE. CARBONYL SULFIDE. DIACETYL. ETHYL FORMATE. NONANE. o-PHTHALODINITRILE. CAS No for piperazine and its salts was ... CYANOGEN. HARD METALS, containing COBALT and TUNGSTEN CARBIDE as Co. ISOBUTYL ACETATE. PROPOXUR. SIMAZINE. TOLUENE DIISOCYANATE ...
  • 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)
  • 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)
  • 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)
  • 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 carbon atom in cyanogen bromide is bonded to bromine by a single bond and to nitrogen by a triple bond (i.e. (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)
  • C98105 Reaction of Imidazoles with Cyanogen Bromide: Cyanation at N 1 or Bromination at C 2? (publish.csiro.au)
  • This project seeks to better characterize the influence of NOM, complexed and uncomplexed Fe and Mn, model and collected pipe deposit material, bromide ion, and oxygen on: 1) the fate of monochloramine and the nature of inorganic reaction products, 2) the kinetics of monochloramine chloramine loss, and 3) the formation of selected organic DBPs. (epa.gov)
  • Because of its simplicity and mild pH conditions, cyanogen bromide activation is the most common method for preparing affinity gels. (wikipedia.org)
  • Bornstein "Structure of alpha-1-CB8, a large cyanogen bromide produced fragment from the alpha-1 chain of rat collagen. (patentgenius.com)
  • Cyanogen produces the second-hottest-known natural flame (after carbon subnitride) with a temperature of over 4,525 °C (8,177 °F) when it burns in oxygen. (wikipedia.org)
  • Cyanogen is the chemical compound with the formula ( C N ) 2 . (wikipedia.org)
  • Cyanogen was first synthesized in 1815 by Joseph Louis Gay-Lussac , who determined its empirical formula and named it. (wikipedia.org)
  • This compound is POISONOUS, and the precautions for cyanogen bromide (above) apply here. (chemicalbook.com)