[Properties and specificity of cathepsin H from the bovine spleen].
Action of cathepsin H from bovine spleen on tuftsin, enkephalin, the oxidized B chain of insulin and a variety of synthetic substrates was studied. Cathepsin H splits off only one N-terminal amino acid from each tuftsin and enkephalin, which, according to the literature, led to inactivation of peptides. The enzyme acts on the oxidized B chain of insulin as an aminoendopeptidase: it splits off the N-terminal phenylalanine and the centrally located bond(s). Km and Vmax for the cathepsin H catalyzed hydrolysis of LeuNA, ArgNA LysNA and BANA were determined. Substrates with the free NH2 group were hydrolyzed at a higher rate. Based on the data obtained and the previously reported results on conversion of kallidin into bradykinin, the specificity of cathepsin H and its possible biological functions were discussed. Cathepsin H appears to participate in formation and inactivation of physiologically active peptides. Using the antiserum to spleen cathepsin H it was found that liver, kidney and lung tissues contained the enzymes identical and/or partially identical to cathepsin H from spleen. The data on the properties of cathepsin H from various sources are summarized.
Lokshina
L A
LA
Lubkova
O N
ON
Gureeva
T A
TA
Orekhovich
V N
VN
D000818:Animals; D056655:Cathepsin H; D002403:Cathepsins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D002417:Cattle; D002855:Chromatography, Thin Layer; D003546:Cysteine Endopeptidases; D000939:Epitopes / Q000032:analysis; D006801:Humans; D006868:Hydrolysis; D005779:Immunodiffusion; D007700:Kinetics; D008970:Molecular Weight; D009928:Organ Specificity; D010455:Peptides / Q000032:analysis; D011817:Rabbits; D051381:Rats; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity
D000939:Epitopes; D010455:Peptides; D002403:Cathepsins; D003546:Cysteine Endopeptidases; C534126:CTSH protein, human; D056655:Cathepsin H; C534128:Ctsh protein, rat
Izuchenie svoĭstv i spetsifichnosti katepsina H iz selezenki byka.