Related Experiment Videos
Purification and characterization of human renal dehydropeptidase I
S Mitsuhashi1, A Fuse, H Mikami
1Episome Institute, Seta Gunma, Japan.
Antimicrobial Agents and Chemotherapy
|April 1, 1988
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.