Purification and characterization of human renal dehydropeptidase I | Zendy

S Mitsuhashi | Zendy; A Fuse | Zendy; Hidetada Mikami | Zendy; Y Saino | Zendy; M. Inoue | Zendy

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Purification and characterization of human renal dehydropeptidase I

Author(s) -

S Mitsuhashi,

A Fuse,

Hidetada Mikami,

Y Saino,

M. Inoue

Publication year - 1988

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.32.4.587

Subject(s) - isoelectric point , chemistry , chromatography , biochemistry , isoelectric focusing , imipenem , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , enzyme , size exclusion chromatography , gel electrophoresis , antibiotics , antibiotic resistance

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.

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