title: Purification and characterization of human renal dehydropeptidase I.
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.
authors.affiliation: Episome Institute, Seta Gunma, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Mitsuhashi
authors.forename: A
authors.initials: A
authors.lastname: Fuse
authors.forename: H
authors.initials: H
authors.lastname: Mikami
authors.forename: Y
authors.initials: Y
authors.lastname: Saino
authors.forename: M
authors.initials: M
authors.lastname: Inoue
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism; D002850:Chromatography, Gel; D004150:Dipeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006868:Hydrolysis; D015378:Imipenem; D007668:Kidney / Q000201:enzymology*; D013845:Thienamycins / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D013845:Thienamycins; D015378:Imipenem; D004150:Dipeptidases; C038937:dipeptidase