Phosphofructokinase in human fetus.

Abstract

The isozymic composition of phosphofructokinase (EC.2.7.1.11) from human fetal tissues has been investigated by immunological characterization, electrophoresis, purification, and SDS-polyacrylamide gel electrophoresis of the dissociated subunits. One of the characteristics of fetal tissues is the indiscriminate expression by all the cells of two or three of the basic forms of phosphofructokinase without any isozyme really corresponding to a specifically fetal form. In particular, L-type enzyme, identical to the highly regulatory enzyme synthesized by the adult hepatocytes, is found in most fetal tissues, especially in muscle and brain. M-type subunits are also detected in most of the organs and constitute the major form in fetal muscle and adrenals. F-type subunits are predominant in fetal stomach and yolk sac and are practically the only form in fetal heart. Some electrophoretic and chromatographic differences between fetal and adult M-type phosphofructokinase exist; whether their nature is genetic or posttraductional is so far unknown. Some differences (of molecular weight and chromatographic properties) are also detected between the fetal L-type subunits and enzyme from adult granulocytes. A mild proteolytic attack of the former by subtilisin transforms it into an enzyme form indistinguishable from granulocyte phosphofructokinase.