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Proteolytic modification of human phosphoglycerate kinase from lymphoblasts
Authors:T.O. Tollefsbol  R.W. Gracy
Affiliation:Departments of Chemistry and Biochemistry, North Texas State University and Texas College of Osteopathic Medicine, Denton, Texas 76203 U.S.A.
Abstract:During phytohemagglutinin and concanavalin A-induced transformation of human lymphocytes, phosphoglycerate kinase (PGK) exhibits new electrophoretic forms (pI = 8.5–8.9). Electrophoresis and electrofocusing showed that the new forms are not due to expression of the autosomally linked isozyme found in sperm (PGK-B; pI = 9.7). The multiple electrophoretic forms are the result of protease modification of the sex-linked PGK-A isozyme.
Keywords:To whom requests for reprints and correspondence should be addressed: Department of Biochemistry   North Texas State University   Denton   Tex. 76203.
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