Biomaterial Database

Peptide esters and nitroanilides as substrates for the assay of human urinary kallikrein. 1978

F Fiedler, and R Geiger, and C Hirschauer, and G Leysath

Ac-Phe-ArgOMe is hydrolyzed much faster than are Bz-ArgOEt, Z-ArgOMe, or Ac-Gly-ArgOMe by the kallikrein from human urine. The synthesis of Ac-Phe-ArgOEt is described. Hydrolysis of this substrate can be conveniently monitored by a coupled spectrophotometric procedure. Increase in absorbance is linear with time and proportional to the amount of kallikrein up to a deltaA366 of at least 0.22/10 min. This assay for human urinary kallikrein is 46-fold more sensitive than that based on Bz-ArgOEt and 38-fold more sensitive than that with D-Val-Leu-Arg-p-nitroanilide. A number of other arginine p-nitroanilides are hydrolyzed by this enzyme at still lower rates. The assay of human urinary kallikrein with D-Val-Leu-ArgOEt is about a factor of two less sensitive than the assay with Ac-Phe-ArgOEt. This also holds for Z-TyrONp, which displays a rapid spontaneous hydrolysis. Furthermore, the rate of the enzymic reaction with Z-TyrONp drops off rapidly.

UI	MeSH Term	Description	Entries
D007610	Kallikreins	Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).	Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D010455	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 considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D004952	Esters	Compounds derived from organic or inorganic acids in which at least one hydroxyl group is replaced by an –O-alkyl or another organic group. They can be represented by the structure formula RCOOR’ and are usually formed by the reaction between an acid and an alcohol with elimination of water.	Ester
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000813	Anilides	Any aromatic amide obtained by acylation of aniline.
D013053	Spectrophotometry	The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities