Pietkiewicz J, Kustrzeba-Wójcicka I, Matusiewicz M, Niemczuk M, Wolna E
Department of Biochemistry, Medical School, Wrocław, Poland.
Acta Biochim Pol. 1991;38(1):139-43.
The treatment of enolase from pig and carp (Cyprinus carpio) with proteases resulted in a decrease of enzymatic activity, which depended on the kind of protease used. The most active were trypsin and subtilisin. Substrate and magnesium ions protected enolase against inactivation. The enolase from pig muscle was much more resistant to protease action than this enzyme from carp muscle. Some differences in the structure between the two enolases are suggested.