Abstract
The presence of acid phosphatase (acid phosphomonoesterase, EC 3.1.3.2) in human red cells was recognized in 1934 (1) and the properties of this enzyme had been studied for almost 30 years (2–7) before its role in human genetics was revealed by Hopkinson et al. (8). The authors examined acid phosphatase from red cell hemolysates by starch-gel electrophoresis. They found two to four active zones, and they distinguished five different red cell acid phosphatase patterns that appeared to be characteristic for the individual and to be genetically determined. In the present work human erythrocytic acid phosphatase was separated into isoenzymes by means of electrofocusing. The isoenzymes were shown to contain increasing numbers of neuraminic acid residues. No genetic variations were observed. Molecular weights of the isoenzymes and their isoelectric points were estimated.
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