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Enzyme Patterns in Human Tissues

IV. Comparison of Glycolytic Enzymes in Surgical Biopsies and Autopsy Specimens¹

Merck, Sharp, and Dohme Research Laboratories, Division of Merck and Company, Inc., Rahway, New Jersey (C.E.S., G.E.B.), and New Jersey College of Medicine and Dentistry, Department of Medicine, Jersey City, New Jersey (H.M., B.J.K.)

Patterns of the glycolytic and some related enzymes were measured in several human tissues obtained surgically and at autopsy. For the most part the enzyme activities were remarkably similar and, hence, when necessary, the determination of these enzymes in specimens obtained at early autopsy is justified. Phosphofructokinase activity, however, was – lower in the tissues obtained at autopsy. The addition of cofactors, such as adenylic acid or adenosine 3',5'-cyclic phosphate did not elevate the activity of phosphofructokinase in specimens obtained at autopsy. Since this enzyme was stable in frozen intact tissues, the loss in activity appears to have occurred prior to autopsy. The reputedly labile glyceraldehyde phosphate dehydrogenase was stable under these conditions. These results show that phosphofructokinase is the 1st enzyme in the glycolytic pathway to lose substantial activity following death.

¹ This investigation was supported by the Cancer Chemotherapy National Service Center, National Cancer Institute, under the NIH, Contracts PH-43-64-883 and PH-43-62-441.

Received 7/26/65.