Modification of membrane protein organization during in vitro aging of human erythrocytes

A. Brovelli, C. Seppi, C. Balduini

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

1. 1. In in vitro aged human erythrocytes, the presence of protein clusters can be found on the membrane; these clusters are made up of peptides held together by disulfide bridges, since they can be nearly completely dissociated by dithiothreitol treatment. 2. 2. SDS-polyacrylamide gel electrophoresis after dithiothreitol dissociation indicates that the aggregates are made of peptide fragments with a molecular weight ranging from 20 to ~ 110 kdalton; none of these fragments correspond to an intact protein component of the membrane. 3. 3. Their formation results from oxidation and proteolysis of membrane, and perhaps cytoplasmic proteins.

Original languageEnglish
Pages (from-to)1115-1120
Number of pages6
JournalInternational Journal of Biochemistry
Volume16
Issue number11
DOIs
Publication statusPublished - 1984

Fingerprint

Erythrocyte Aging
Dithiothreitol
Membrane Proteins
Aging of materials
Membranes
Peptide Fragments
Disulfides
Proteolysis
Polyacrylamide Gel Electrophoresis
Proteins
Erythrocytes
Molecular Weight
Cell Membrane
Electrophoresis
Peptides
Molecular weight
Oxidation
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

Cite this

Modification of membrane protein organization during in vitro aging of human erythrocytes. / Brovelli, A.; Seppi, C.; Balduini, C.

In: International Journal of Biochemistry, Vol. 16, No. 11, 1984, p. 1115-1120.

Research output: Contribution to journalArticle

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