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 dehydropeptidase I hydrolyzed imipenem, carpetimycins A and B, and Sch 29,482.
Mitsuhashi
S
S
Episome Institute, Seta Gunma, Japan.
Fuse
A
A
Mikami
H
H
Saino
Y
Y
Inoue
M
M
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
D000900:Anti-Bacterial Agents; D013845:Thienamycins; D015378:Imipenem; D004150:Dipeptidases; C038937:dipeptidase