[Isolation and properties of neutral SH-dependent proteinase from bovine spleen].
A neutral SH-dependent proteinase was isolated from bovine spleen by a slight modification of the previous method (1) and its action on some natural and synthetic substrates was studied. The activity of the enzyme was increased 2000--2500-fold as compared to that of the original extract. The enzyme hydrolyzed various histones (H1, H2a, H2b, H3), casein and protamine but did not split hemoglobin, serum albumin and 14C-tryptophane-labelled total protein from chicken embryos. The enzyme possessed neither collagenolytic nor elastase activity; it did not inactivate aldolase, hexokinase, glyceraldehyde phosphate dehydrogenase and glucose-6-phosphate dehydrogenase, which makes the enzyme different from cathepsin B1 and some other previously described proteinases. The enzyme did not split BAPA, BAEE, ATEE, Boc-Ala-ONP, Leu-beta-NA and some other peptides. The molecular weight of the enzyme was found to be about 15 000.
D000818:Animals; D002417:Cattle; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D013438:Sulfhydryl Compounds; D010450:Endopeptidases
Vydelenie i svoĭstva neĭtral'noĭ SH-3avisimoi proteina3y sele3enki byka.