抄録
Angiotensin I-converting enzyme of hog kidney exists in two different forms, peak A and peak B, as shown by hydroxyapatite column chromatography. These enzymes were found to possess identical molecular weights by filtration through Sephadex G-200. The sialic acid and neutral sugar contents of peak A were roughly twice those of peak B. The peak A preparation gave a single protein component on SDS-gel electrophoresis, while peak B showed three components. After neuraminidase treatment, however, both enzyme preparations showed a single protein band with an estimated molecular weight of 90000 as determined by SDS-gel electrophoresis. It is suggested that the different mobilities of the two forms on electrophoresis depend upon the relative amounts of sialic acid in their molecules, and that these enzymes consist of two polypeptide chains.
