Angiotensin-converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties.

摘要: Angiotensin-converting enzyme was purified from human lung, kidney, testis, blood plasma, and seminal plasma using a facile two-step protocol which included affinity chromatography on Sepharose-bound lisinopril followed by either gel filtration or hydroxylapatite chromatography. Molecular mass for converting all sources except testis 140 kDa. That consisted of both 90- 140-kDa form in 4:1 ratio. Detergent-extracted membrane-bound aggregated chromatography, while trypsin-extracted soluble did not. Comparison detergent-extracted sodium dodecyl sulfate-polyacrylamide electrophoresis isoelectric focusing indicated that the membrane binding sequence contributed minimally to size charge enzyme. Catalytic kinetic properties assessed interaction with substrates, inhibitors, anti-converting immunoglobulin were similar forms Enzyme-linked immunosorbent assay revealed only partial homology between