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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Bibliografiske detaljer

Udgivet i:	Antimicrob Agents Chemother
Principais autores:	Mitsuhashi, S, Fuse, A, Mikami, H, Saino, Y, Inoue, M
Format:	Artigo
Sprog:	Inglês
Udgivet:	American Society for Microbiology (ASM) 1988
Fag:	Research Article
Online adgang:	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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