Studies on the Ca2+-Activated Neutral Proteinase of Rabbit Skeletal Muscle. I. The Characterization of the 80 K and the 30 K Subunits

Publisher Website
Google Scholar
Abstract
The structure of the calcium-activated neutral proteinase (CANP) from rabbit skeletal muscle was examined. The purified CANP was homogeneous as judged by disc gel electrophoresis, while it showed two bands (M.W.=80,000 (80 K) and 31,000 (30 K)) on SDS-gel electrophoresis. After denaturation of CANP, each subunit was separated and could be renatured alone or in combination with the other sub-unit. The results indicated that all the machinary necessary for the proteolytic activity is present in the 80 K subunit, but for the full activity the existence of the 30 K subunit is required.