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.