| Literature DB >> 3163907 |
S Mitsuhashi1, A Fuse, H Mikami, Y Saino, M Inoue.
Abstract
Dehydropeptidase I from human kidney was purified over 100-fold. The purified enzyme had an isoelectric point of 4.75, apparent molecular weights of 135,000 by gel filtration and of 66,500 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and an optimal pH of 7.4. Human renal dehydropeptidase I hydrolyzed imipenem, carpetimycins A and B, and Sch 29,482.Entities:
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Year: 1988 PMID: 3163907 PMCID: PMC172226 DOI: 10.1128/AAC.32.4.587
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191