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Literature DB >> 7188423

The isolation of human-erythrocyte band-3 polypeptide labelled with a photosensitive hydrophobic probe.

Abstract

To investigate the intramembranous domains of the major band-3 polypeptide, human erythrocyte membranes were labelled with 1-azido-4-[125I]iodobenzene. The anion-exchange protein has been isolated by a new procedure that decreases possible contamination by other integral membrane proteins of similar molecular weight. After chemical modification, the protein was subjected to proteolytic cleavage by several proteinases to yield a distinct pattern of peptides, a few of which contained radioactivity.

Entities: Chemical Species

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Year: 1980 PMID： 7188423 PMCID： PMC1162456 DOI： 10.1042/bj1870719

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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References

29 in total

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Authors: R E Jenkins; J A Tanner
Journal: Biochem J Date: 1975-06 Impact factor: 3.857

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Authors: Z I Cabantchik; A Rothstein
Journal: J Membr Biol Date: 1974 Impact factor: 1.843

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Authors: J V Staros; F M Richards
Journal: Biochemistry Date: 1974-06-18 Impact factor: 3.162

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Authors: M S Bretscher
Journal: Nat New Biol Date: 1971-06-23

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Authors: J B Findlay
Journal: J Biol Chem Date: 1974-07-25 Impact factor: 5.157

10. A new approach to the study of phospholipid-protein interactions in biological membranes. Synthesis of fatty acids and phospholipids containing photosensitive groups.

Authors: P Chakrabarti; G Khorana
Journal: Biochemistry Date: 1975-11-18 Impact factor: 3.162

The isolation of human-erythrocyte band-3 polypeptide labelled with a photosensitive hydrophobic probe.

1. The major human erythrocyte membrane protein. Evidence for an S-shaped structure which traverses the membrane twice and contains a duplicated set of sites.

2. A membrane protein from human erythrocytes involved in anion exchange.

3. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.

4. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate.

5. Photoactive covalent labeling of membrane components from within the lipid core.

6. Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation.

7. Photochemical labeling of the surface proteins of human erythrocytes.

8. Major human erythrocyte glycoprotein spans the cell membrane.

9. The receptor proteins for concanavalin A and Lens culinaris phytohemagglutinin in the membrane of the human erythrocyte.

10. A new approach to the study of phospholipid-protein interactions in biological membranes. Synthesis of fatty acids and phospholipids containing photosensitive groups.