Abstract
Abstract Human plasma and serum acid phosphatases are studied by biochemical methods to evaluate the total enzyme activity and by polyacrylamide gel electrophoresis to demonstrate the isoenzyme patterns. The aim is to identify the tissue or cell origin of the various isoenzymes in plasma. Normal plasma contains a tartrate-resistant isoenzyme 5 but no demonstrable isoenzymes from red blood cells or prostate. Normal serum contains an additional isoenzyme 3 which is tartrate-sensitive and is released from platelets during blood clotting. In a variety of diseases, other isoenzymes may appear in plasma. In metastatic prostate cancer, for example, the changes of plasma enzyme activity are due to the presence of isoenzyme 2. Many acid phosphatase isoenzymes are cell-specific, i.e., derived from a specific type of cell. Abnormal enzyme activity and zymogram patterns of plasma acid phosphatase frequently reflect those of tissues in disease conditions. In some of the cases with abnormal plasma acid phosphatase isoenzymes, the total enzyme activity in plasma is normal. Results of this study suggest that examination of the isoenzymes by gel electrophoresis is more sensitive than the biochemical methods in tracing the cause responsible for the enzyme changes in plasma.
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