Human erythrocyte membrane enzymes [letter]

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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...

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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 ...

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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...

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Association of glycolytic enzymes with the erythrocyte membrane.

Fraker, P. J. & Speck, J. C., Jr. (1978) Biochem. Biophys. Res. Snary, D., Goodfellow, P., Hayman, M. J., Bodmer, W. F. & Commun. 80,849-857 Hubbard, A. L. & Cohn, 2. A. (1976) in Biochemical Analysis of Okayama, H., Ueda, K. & Hayaishi, 0. (1978) Proc. Natl. Acad. Sci. Membranes (Maddy, A. H., ed.), pp. 427-501, Chapman and Hall, London Zittle, C. A. (1951) Adv. Enzymol. Relat. Areas Mol. Biol...

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Arrangement of human erythrocyte membrane proteins.

The orientation of human erythrocyte membrane protein was examined by enzymic iodination using lactoperoxidase with the glucose-oxidase system for generating peroxide, followed by proteolytic digestion. The outer surface of intact cells was labeled with 125I and the cytoplasmic surface of either resealed ghosts containing lactoperoxidase or of inside-out vesicles was labeled with 131I. Followin...

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ژورنال

عنوان ژورنال: Blood

سال: 1978

ISSN: 0006-4971,1528-0020

DOI: 10.1182/blood.v51.2.367.367