ENZYMES OF THE HUMAN ERYTHROCYTE

Enzymes of the Human Erythrocyte

The enzymatic interconversion involves a net transfer of hydrogen which migrates as a proton (1). In spite of an early reference (2) to the role and existence of this glycolytic enzyme within a variety of animal tissues, it apparently has not been prepared previously in a significantly purified state from any source. Fractions rich in this enzyme have been separated from rabbit muscle (3), and ...

Enzymes of the Human Erythrocyte

A detailed description of appropriate procedures for the isolation in presumably ahnost pure form of a purine nucleoside phosphorylase from human erythrocytes was presented as the original report of Paper I (1). The present paper will s ummarize the results of investigations concerning the stability characteristics and kinetic properties of the isolated enzyme. Enzymatic degradation of nucleosi...

Human erythrocyte membrane enzymes: current status and clinical correlates.

By Stanley L. Schrier T HE PAST TWENTY YEARS have seen a remarkable growth in information concerning the metabolism of the human erythrocyte. It became apparent that, depending on the method of preparation, some of the enzymes of the human erythrocyte can be recovered partially or totally in an operationally defined membrane fraction. Therefore, there now exists a substantial body of informatio...

Erythrocyte Antioxidant Enzymes in Hyperlipoproteinemia

Erythrocyte glucose 6-phosphate dehydrogenase of normal and mutant human subjects: properties of the purified enzymes.

A deficiency in human erythrocyte glucose 6-phosphate dehydrogenase may be genetically determined (l-4) or occur in normal erythrocytes as they age in tivo (5, 6). The inherited glucose-6-P dehydrogenase deficiency, which is associated with hemolytic anemia upon exposure to a variety of agents, affords an opportunity in man to study further the mechanisms by which genes can lead to a decrease i...