Open AccessHuman, rabbit, bovine, and porcine creatine kinase isoenzymes are glycoproteins
Author(s) -
McBride James H,
McBride James H,
Rodgerson Denis O,
Hilborne Lee H.
Publication year - 1990
Publication title -
journal of clinical laboratory analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 50
eISSN - 1098-2825
pISSN - 0887-8013
DOI - 10.1002/jcla.1860040310
Subject(s) - isozyme , creatine kinase , isoelectric focusing , glycoprotein , biochemistry , protein subunit , carbohydrate , isoelectric point , enzyme , chemistry , microbiology and biotechnology , catabolism , biology , gene
Abstract Human, rabbit, bovine, and porcine creatine kinase (CK) isoenzyme preparations were extensively purified by isoelectric focusing and high‐performance liquid chromatography and tested for the presence of carbohydrate. In this study, all the CK isoenzymes demonstrated positive periodic acid‐Schiff (PAS) reactions, indicating the presence of carbohydrate. It is concluded that CK is a glycoprotein as a carbohydrate, associated with the M subunit of human, rabbit, bovine, and porcine isoenzymes. Also, carbohydrate is an integral part of the B subunit of both rabbit brain and porcine heart CK. Loss of carbohydrate may be important in enzyme catabolism, yielding a pool of circulating modified CK protein that, to date, has remained undetected by traditional methods.