The bovine lens neutral proteinase comprises a family of cysteine-dependent proteolytic activities
作者:
WagnerB. J.,
MargolisJoyce W.,
AbramovitzAaron S.,
期刊:
Current Eye Research
(Taylor Available online 1986)
卷期:
Volume 5,
issue 11
页码: 863-868
ISSN:0271-3683
年代: 1986
DOI:10.3109/02713688609029238
出版商: Taylor&Francis
数据来源: Taylor
摘要:
Inhibitor studies with peptide substrates demonstrate that bovine lens neutral proteinase comprises three distinct activities. Diisopropylfluoro-phosphate distinguishes the activity hydrolyzing carbobenzoxy-Gly-Gly-Leu-p-nitroanilide (inhibited) from that hydrolyzing carbobenzoxy-Leu-Leu-Glu-2-naphthylamide (not inhibited). Leupeptin inhibits hydrolysis of the substrate carbobenzoxy-Leu-Leu-Arg-2-naphthylamide, but not hydrolysis of car-bobenzoxy-Gly-Gly-Leu-p-nitroanilide or carbobenz-oxy-Leu-Leu-Glu-2-naphthylamide, demonstrating the presence of the third activity. Inhibition of the three activities by thiol reagents suggests that each activity may be dependent on an active-site cysteine residue.
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