Purification and characterization of human renal dehydropeptidase I.

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 dehydropept...

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Vydáno v:	Antimicrob Agents Chemother
Hlavní autoři:	Mitsuhashi, S, Fuse, A, Mikami, H, Saino, Y, Inoue, M
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1988
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC172226/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3163907/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.32.4.587
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