Work

Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase.

Year: 1982

Type: article

Abstract: Band 3, the anion transport protein of the human erythrocyte, provides the site of association of certain glycolytic enzymes with the membrane. We have now demonstrated that glyceraldehyde-3-P dehydrogenase is inhibited, reversibly and completely, when membrane bound. The inhibition was competitive with respect to NAD+ and arsenate, but was noncompetitive with glyceraldehyde-3-P. Peptide fragments containing the NH2-terminal 23 residues of band 3 also inhibited the enzyme and displaced it from ghosts. Thus, the red cell membrane binding site for glyceraldehyde-3-P dehydrogenase is the same as that for aldolase, the polyanionic NH2-terminal region of the band 3 polypeptide.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)68212-8

Authors: I.H. Tsai, S.N. Murthy, T.L. Steck

Institutions: University of Chicago, Institute of Biological Chemistry, Academia Sinica, Academia Sinica

Language: English

Topic: Erythrocyte Function and Pathophysiology

Subfield: Physiology (medical)

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430