A chromogenic substrate that permits direct measurement of peptide hydrolase activity, e.g., papain and trypsin, by colorimetry. The substrate liberates p-nitroaniline as a chromogenic product.
The simplest of all peptides. It functions as a gamma-glutamyl acceptor.
Anilides are organic compounds resulting from the reaction of aniline (a primary aromatic amine) with carboxylic acids or their derivatives, forming amides, which have various applications in pharmaceuticals and agrochemicals.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The rate dynamics in chemical or physical systems.

Inhibition of human and ovine acrosomal enzymes by tannic acid in vitro. (1/25)

The effect of tannic acid, a common flavonoid, on the acrosin and plasminogen activator activity and plasmin activity of human and ram spermatozoa was evaluated. Acrosin and plasminogen activator activity were determined by spectrophotometry using the chromogenic substrates N-alpha-benzoyl-DL-arginine para-nitroanilide-HCl (BAPNA) and H-D-valyl-L-leucyl-L-lysine-p-nitroanilide-2HCl (S-2251), respectively. In extracts from both human and ovine acrosomes, the activities of acrosin and plasminogen activators were susceptible to tannic acid inhibition. The inhibitory effect of tannic acid was observed at concentrations > 50 micromol l(-1) in a dose-dependent manner. In additional experiments, low concentrations of tannic acid significantly inhibited tissue-type plasminogen activator, urokinase-type plasminogen activator and plasmin activity in a concentration-dependent manner over the range 0.25-200 micromol l(-1). Tannic acid reduced the motility of ram spermatozoa at a concentration of 1000 micromol l(-1) after 2 and 3 h co-incubation with spermatozoa. The motility of human spermatozoa remained unchanged over the range 0.1-1000 micromol tannic acid l(-1) during 3 h co-incubation. These results indicate that tannic acid inhibited the activity of both acrosin and plasminogen activator and indicates a possible mechanism by which flavonoids exert their antifertility effects.  (+info)

Isolation and characterization of an alpha-macroglobulin from the gastropod mollusc Helix pomatia with tetrameric structure and preserved activity after methylamine treatment. (2/25)

A proteinase inhibitor with M(r) 697000 and 20.3% (w/w) carbohydrate was isolated from the haemolymph of the snail Helix pomatia and characterized. It was shown to have a tetrameric structure with subunits disulphide linked by two. It inhibited the activity of several types of proteinases against large substrates but not that of trypsin against N-alpha-benzoyl-DL-arginine-4-nitroanilide. This indicated a nonspecific and steric hindrance mode of inhibition. The ratio of trypsin molecules inactivated per inhibitor amounted to 1.5. This interaction led to a cleavage of the subunits into two equal fragments and to a slow to fast conformational change of the whole molecules. Experiments with 125I-labelled trypsin indicated that the proteinase had become covalently linked to one of the fragments. Heating of the inhibitor led to autolytic cleavage products but not when methylamine treated. Thiol titration after trypsin or methylamine treatment indicated the presence of one thiol ester bond per subunit. These facts are all indicative of an alpha-macroglobulin type of inhibitor. However, unlike for most of them the methylamine treatment did not induce a conformational change nor suppress its proteinase inhibitory activity. Moreover, invertebrate alpha-macroglobulins are mostly dimeric in structure but tetramers likewise do occur in Biomphalaria glabrata.  (+info)

Preparation of fully active ficin from Ficus glabrata by covalent chromatography and characterization of its active centre by using 2,2'-depyridyl disulphide as a reactivity probe. (3/25)

1. Fully active ficin (EC 3.4.22.3) containing 1 mol of thiol with high reactivity towards 2,2'-dipyridyl disulphide (2-Py-S-S-2-Py) at pH4.5 per mol of protein was prepared from the dried latex of Ficus glabrata by covalent chromatography on a Sepharose-glutathione-2-pyridyl disulphide gel. 2. Ficin thus prepared is a mixture of ficins I-IV and ficin G, in which ficins II and III predominate. The various ficins exhibit similar reactivity characteristics towards 2-Py-S-S-2-Py. 3. Use of 2-Py-S-S-2-Py as a reactivity probe demonstrates (a) that in ficin, as in papain (EC 3.4.22.2), the active-centre thiol and imidazole groups interact to provide a nucleophilic state at pH values of approx. 6 additional to the uncomplicated thiolate ion that predominates at pH values over 9, and (b) a structural difference between ficin and papain that leads to a much higher rate of reaction of 2-Py-S-S-2-Py with ficin than with papain at pH values 3-4. This difference is suggested to include a lack in ficin of a carboxyl group conformationally equivalent to that of aspartic acid-158 in papain. 4. The high electrophilicity of the 2-Py-S-S-2PyH+ monocation allows directly the detection of the exposure of the buried thiol group of ficin at pH values below 4.  (+info)

Evidence that Fitzgerald factor counteracts inhibition by kaolin or ellagic acid of the amidolytic properties of a plasma kallikrein. (4/25)

Fitzgerald trait, an asymptomatic disorder, is associated with abnormalities of surface-mediated plasma reactions, including coagulation via the intrinsic pathway, augmentation of the clot-promoting properties of factor VII, kaolin-mediated fibrinolysis, kinin generation, and enhancement of vascular permeability by diluted plasma (PF/Dil). These abnormalities can be corrected by Fitzgerald factor, an agent probably identical with high molecular weight kininogen found in normal, but not Fitzgerald-trait plasma. Our preparations of Fitzgerald factor possessed a second property. Amidolysis of alpha-N-benzoyl-L-proline-L-phenylalanine-L-arginine-pnitroanilide by a plasma kallikrein (activated Fletcher factor) was inhibited by kaolin or solutions of ellagic acid. Addition of preparations of Fitzgerald factor to kaolin or to solutions of ellagic acid counteracted their inhibitory properties. The action of these preparations was duplicated by solutions of cytochrome C or IgG, suggesting that these agents may inhibit the negative charges of kaolin or ellagic acid. Fitzgerald factor enhanced amidolysis of both normal and Fitzgerald-trait plasmas exposed to kaolin, effects not duplicated by cytochrome C or IgG. Whether or not the two properties of our preparations of Fitzgerald factor are related to the same agent is not yet certain. The relationship between these observations and the biologic role of Fitzgerald factor remains to be investigated.  (+info)

Evidence for independent molecular identity and functional interaction of the haemagglutinin and cysteine proteinase (gingivain) of Porphyromonas gingivalis. (5/25)

The sequence of events involved in haemagglutination and lysis of erythrocytes by washed cells, vesicles and the culture supernate of Porphyromonas gingivalis strain W83 was monitored by 51Cr release and transmission electronmicroscopy. All preparations, except capsular material and lipopolysaccharide, caused haemagglutination and, by a slow process of attachment and specific attack on the surface structures of the red blood cells, produced minute pores and eventual leakage of cellular contents. N-acetylglucosamine, N-acetylgalactosamine and several other sugars such as glucose and sucrose had no effect on haemagglutination. Antiserum raised against a cloned haemagglutinin of P. gingivalis strain 381 inhibited the activity of strain W83 cells, vesicles and supernate. The antiserum-neutralised supernate lost 70-80% of its hydrolytic activity towards alpha-N-benzoyl-L-arginine-4-nitroanilide but the residual activity behaved in a manner similar to the native supernate in that it was completely inhibited by the addition of 2,2'-dipyridyl disulphide and was fully restored upon addition of a low-Mr mercaptan. Binding of the antiserum to the haemagglutinin epitope of P. gingivalis still permitted titration of the active centre cysteinyl thiol group of the proteinase. Purified gingivain caused lysis of erythrocytes and was not neutralised by antiserum to the haemagglutinin. These results suggest that, although the haemagglutinin and gingivain are probably separate molecules, they are closely associated on the outer membrane of P. gingivalis and may be functionally related.  (+info)

Separation, purification and N-terminal sequence analysis of a novel leupeptin-sensitive serine endopeptidase present in chemically induced rat mammary tumour. (6/25)

Leupeptin is a small peptide microbially derived inhibitor of certain proteolytic enzymes. Using N-alpha-benzoyl-DL-arginine 4-nitroanilide as substrate, we found a novel leupeptin-sensitive proteolytic enzyme in N-methyl-N-nitrosourea(MNU)-induced rat mammary adenocarcinoma. This enzyme was apparently different from urokinase-type plasminogen activator or cathepsin B and was present in mammary tumour at levels at least 20 times higher than those in normal mammary tissue. This enzyme was separated and purified from crude extracts of MNU-induced mammary adenocarcinoma approx. 1900-fold with 34% yield. It was a trypsin-like serine endopeptidase and had a pH optimum at 7.0. The native enzyme had an apparent M(r) of 180,000 and exhibited four isoelectric points ranging from 4.3 to 5.0. Electrophoresis of denatured enzyme, however, yielded, with reduction, a major band with an apparent M(r) of 37,500 and a minor band with an apparent M(r) of 35,500. The N-terminal 23 residues of the major band were Ile1-Val2-Gly3-Gly4-Gln5-Glu6-Ala7-+ ++Ser8-Gly9-Asn10-Lys11-Xaa12-Pro13- Val14- Gln15-Val16-Xaa17-Leu18-Xaa19-Val20- Trp21-Leu22-Pro23. These and other properties of this enzyme suggested that it most closely resembles rat skin tryptase, followed by rat peritoneal mast-cell tryptase and then by tryptases from other species. The rat, like human and mouse, may carry multiple tryptase genes, and this mammary-tumour enzyme may be an additional form of rat tryptase within a new serine-proteinase family.  (+info)

Studies on the catalytic action of poly-alpha-amino acids. VII. Stereospecificity in the enzyme-like hydrolysis of benzoyl-L-(D)-arginine-p-nitroanilides by copoly (Cys, Glu). (7/25)

The substrate specificity in the hydrolysis of L-, DL-, and D-BAPA (benzoylarginine-p-nitro-anilide) by copoly (L-Cys, L-Glu) and copoly (D-Cys, D-Glu) was studied, and enzyme-like stereospecific hydrolyses by poly-alpha-amino acids were identified for the first time. The L-type copolymer hydrolyzed L-BAPA faster than D-BAPA and the rates (v) of BAPA hydrolyses by L-type copolymer were found to be in the order vL greater than vDL greater than vD. On the other hand, the D-type copolymer hydrolysed D-BAPA faster than L-BAPA and the rates of BAPA hydrolyses by D-type copolymer were in the order vD greater than vDL greater than vL. In all cases, the reaction followed Michaelis-Menten kinetics when the substrate concentration was corrected, and the optimum conditions of the reaction were pH 6.0 and 40 degrees. The activity appeared after a certain amount of BAPA had combined with the polymer. D- and L-substrates combine competitively with the polymer and the different rates of hydrolysis are presumably due to the different substrate configurations in relation to the conformation of the active site in the polymer. The polymer shows activity near the range of random coil conformation, where some alpha-helical conformation is still present. Only some of the cysteine residues in the copolymer are involved in the hydrolytic activity.  (+info)

Overexpression and mechanistic characterization of blastula protease 10, a metalloprotease involved in sea urchin embryogenesis and development. (8/25)

Blastula protease 10 (BP10) is a metalloenzyme involved in sea urchin embryogenesis, which has been assigned to the astacin family of zinc-dependent endopeptidases. It shows greatest homology with the mammalian tolloid-like genes and contains conserved structural motifs consistent with astacin, tolloid, and bone morphogenetic protein 1. Astacin, a crustacean digestive enzyme, has been proposed to carry out hydrolysis via a metal-centered mechanism that involves a metal-coordinated "tyrosine switch." It has not been determined if the more structurally complex members of this family involved in eukaryotic development share this mechanism. The recombinant BP10 has been overexpressed in Escherichia coli, its metalloenzyme nature has been confirmed, and its catalytic properties have been characterized through kinetic studies. BP10 shows significant hydrolysis toward gelatin both in its native zinc-containing form and copper derivative. The copper derivative of BP10 shows a remarkable 960% rate acceleration toward the hydrolysis of the synthetic substrate N-benzoyl-arginine-p-nitroanilide when compared with the zinc form. The enzyme also shows calcium-dependent activation. These are the first thorough mechanistic studies reported on BP10 as a representative of the more structurally complex members of astacin-type enzymes in deuterostomes, which can add supporting data to corroborate the metal-centered mechanism proposed for astacin and the role of the coordinated Tyr. We have demonstrated the first mechanistic study of a tolloid-related metalloenzyme involved in sea urchin embryogenesis.  (+info)

Benzoylarginine nitroanilide is a synthetic peptide derivative that is often used as a substrate in enzyme assays, particularly for testing the activity of proteases (enzymes that break down proteins). Proteases cleave the peptide bond between benzoyl and arginine in the molecule, releasing p-nitroaniline, which can be easily measured spectrophotometrically. This allows researchers to quantify the activity of protease enzymes in a sample. It is also known as Benzoyl-L-arginine ρ-nitroanilide hydrochloride or BAPNA.

Glycylglycine is not a medical condition or term, but rather it is a chemical compound. It is a dipeptide, which means it is composed of two amino acids linked together. Specifically, glycylglycine consists of two glycine molecules joined by an amide bond (also known as a peptide bond) between the carboxyl group of one glycine and the amino group of the other glycine.

Glycylglycine is often used in laboratory research as a buffer, a substance that helps maintain a stable pH level in a solution. It has a relatively simple structure and is not naturally found in significant amounts in living organisms.

Anilides are chemical compounds that result from the reaction between aniline (a organic compound with the formula C6H5NH2) and a carboxylic acid or its derivative. The resulting compound has the general structure R-CO-NH-C6H5, where R represents the rest of the carboxylic acid molecule.

Anilides are widely used in the pharmaceutical industry to produce various drugs, such as analgesics, anti-inflammatory agents, and antifungal agents. Some examples of anilide-based drugs include acetaminophen (also known as paracetamol), fenacetin, and flufenamic acid.

It's worth noting that some anilides have been found to have toxic effects on the liver and kidneys, so they must be used with caution and under medical supervision.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

In enzymology, a D-benzoylarginine-4-nitroanilide amidase (EC 3.5.1.72) is an enzyme that catalyzes the chemical reaction N- ... "Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide". J. ... The systematic name of this enzyme class is N-benzoyl-D-arginine-4-nitroanilide amidohydrolase. Other names in common use ... the two substrates of this enzyme are N-benzoyl-D-arginine-4-nitroanilide and H2O, whereas its two products are N-benzoyl-D- ...
... benzoylarginine-2-naphthylamide MeSH D12.125.068.050.100 - benzoylarginine nitroanilide MeSH D12.125.068.050.400 - homoarginine ... benzoylarginine-2-naphthylamide MeSH D12.125.095.104.100 - benzoylarginine nitroanilide MeSH D12.125.095.104.400 - homoarginine ...
... benzoylarginine nitroanilide MeSH D02.065.199.239 - bupivacaine MeSH D02.065.199.326 - carbanilides MeSH D02.065.199.326.400 - ...
D-benzoylarginine-4-nitroanilide amidase EC 3.5.1.73: carnitinamidase EC 3.5.1.74: chenodeoxycholoyltaurine hydrolase EC 3.5. ...
In enzymology, a D-benzoylarginine-4-nitroanilide amidase (EC 3.5.1.72) is an enzyme that catalyzes the chemical reaction N- ... "Bacteria of the genus Bacillus have a hydrolase stereospecific to the D isomer of benzoyl-arginine-p-nitroanilide". J. ... The systematic name of this enzyme class is N-benzoyl-D-arginine-4-nitroanilide amidohydrolase. Other names in common use ... the two substrates of this enzyme are N-benzoyl-D-arginine-4-nitroanilide and H2O, whereas its two products are N-benzoyl-D- ...
Benzoylarginine Nitroanilide, Monosodium Salt, Monohydrochloride*Benzoylarginine Nitroanilide, Monosodium Salt, ... "Benzoylarginine Nitroanilide" by people in this website by year, and whether "Benzoylarginine Nitroanilide" was a major or ... Benzoylarginine Nitroanilide Monohydrochloride*Benzoylarginine Nitroanilide Monohydrochloride. *Monohydrochloride, ... "Benzoylarginine Nitroanilide" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ...
Benzoylarginine Nitroanilide. *Bupivacaine. *Carbanilides. *Carboxin. *Encainide. *Flutamide. *Prilocaine. *Propanil. * ...
Benzoyl-arginine-p-nitroanilide (Bz-Arg-pNan) was hydrolyzed by the saline extract. ...
... benzoyl-arginine-p-nitroanilide (BAPA) [11]. The activity of D-BAPA-ase was highest at low NaCl concentration (100 mM) and ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide [D02.092.146.113.200] * Bupivacaine [D02.092.146.113.239] * Levobupivacaine [D02.092.146.113. ...
Benzoylarginine-2-Naphthylamide [D12.125.068.050.095] * Benzoylarginine Nitroanilide [D12.125.068.050.100] * Homoarginine [ ... Benzoylarginine 2 Naphthylamide Benzoylarginine beta-Naphthylamide Registry Number. 305-09-9. CAS Type 1 Name. Benzamide, N-(4 ... use BENZOYLARGININE-2-NAPHTHYLAMIDE to search BENZOYLARGININE BETA NAPHTHYLAMIDE 1976. History Note. 91(77); was see under ... Benzoylarginine-2-Naphthylamide Preferred Term Term UI T004593. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide, (R)-Isomer Benzoylarginine Nitroanilide, (S)-Isomer Benzoylarginine Nitroanilide, Monosodium Salt ... N-Benzoylarginine-4-nitroanilide N-Benzoylarginyl-4-nitroanilide N-alpha-Benzoyl-DL-arginine-4-nitroanilide Pharm Action. ... Benzoylarginine Nitroanilide, (S)-Isomer Related Concept UI. M0330839. Registry Number. 6208-93-1. Terms. Benzoylarginine ... Benzoylarginine Nitroanilide, (R)-Isomer Related Concept UI. M0330838. Registry Number. 26056-64-4. Terms. Benzoylarginine ...
Benzoylarginine Nitroanilide, (R)-Isomer Benzoylarginine Nitroanilide, (S)-Isomer Benzoylarginine Nitroanilide, Monosodium Salt ... N-Benzoylarginine-4-nitroanilide N-Benzoylarginyl-4-nitroanilide N-alpha-Benzoyl-DL-arginine-4-nitroanilide Pharm Action. ... Benzoylarginine Nitroanilide, (S)-Isomer Related Concept UI. M0330839. Registry Number. 6208-93-1. Terms. Benzoylarginine ... Benzoylarginine Nitroanilide, (R)-Isomer Related Concept UI. M0330838. Registry Number. 26056-64-4. Terms. Benzoylarginine ...
D-benzoylarginine-4-nitroanilide amidase (substance). Code System Preferred Concept Name. D-benzoylarginine-4-nitroanilide ...
N-Benzoylarginine-4-nitroanilide N-Benzoylarginyl-4-nitroanilide Nitroanilide, Benzoylarginine Benzoylarginine Nitroanilide, (S ... Benzoylarginine Nitroanilide, (R)-Isomer. Benzoylarginine Nitroanilide, (S)-Isomer. Benzoylarginine Nitroanilide, Monosodium ... Benzoylarginine Nitroanilide Entry term(s). BAPNA N Benzoylarginine 4 nitroanilide N Benzoylarginyl 4 nitroanilide ... N-Benzoylarginine-4-nitroanilide. N-Benzoylarginyl-4-nitroanilide. N-alpha-Benzoyl-DL-arginine-4-nitroanilide. Nitroanilide, ...
N0000166943 Benzoxepins N0000005968 Benzoyl Peroxide N0000170233 Benzoylarginine Nitroanilide N0000170229 Benzoylarginine-2- ...
INDICATORS AND REAGENTS BENZOYLARGININE NITROANILIDE INDICATORS AND REAGENTS BIURET INDICATORS AND REAGENTS BROMCRESOL GREEN ... CHOLINESTERASE REACTIVATORS BENZOYLARGININE NITROANILIDE CHROMOGENIC COMPOUNDS CHROMOGENIC COMPOUNDS CHROMOGENIC COMPOUNDS 6- ...
Benzoylarginine Nitroanilide D2.92.146.113.200 Benztropine D4.75.80.875.99.722.270 D3.605.84.500.722.270 Benzydamine D3.438. ...
Benzoylarginine Nitroanilide [D02.065.199.200] * Bupivacaine [D02.065.199.239] * Carbanilides [D02.065.199.326] * Carboxin [ ...
Benzoylarginine-2-Naphthylamide [D12.125.068.050.095] * Benzoylarginine Nitroanilide [D12.125.068.050.100] * Homoarginine [ ...

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