Protein 4.1

Its association with the human erythrocyte membrane

K. A. Shiffer, Steven Goodman

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

125I-labeled protein 4.1a and 4.1b have equal ability to reassociate with inside-out erythrocyte vesicles that were depleted of protein 4.1 in addition to other peripheral membrane proteins. The reassociation of 125I-labeled protein 4.1 to protein 4.1-depleted vesicles at 4°C is salt dependent, pH dependent, and saturable with a K(d) of 42-50 nM and an extrapolated maximal binding capacity of 120-140 μg of protein 4.1 bound per mg of vesicle protein or 60-70 μg of protein 4.1 bound per mg of ghost protein, correlating with the protein 4.1 content in the erythrocyte membrane (6-7% of the total membrane protein). Selective proteolytic cleavage of these vesicles with papain (5 μg/ml at 4°C) eliminates > 60% of the high-affinity binding sites; therefore, we conclude that the interaction of protein 4.1 with the cytoplasmic membrane surface is through a specific high-affinity protein-protein association.

Original languageEnglish (US)
Pages (from-to)4404-4408
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume81
Issue number14 I
DOIs
StatePublished - Jan 1 1984

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Erythrocyte Membrane
Proteins
Membrane Proteins
Papain
Salts
Erythrocytes
Binding Sites
Cell Membrane

All Science Journal Classification (ASJC) codes

  • General

Cite this

Protein 4.1 : Its association with the human erythrocyte membrane. / Shiffer, K. A.; Goodman, Steven.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 81, No. 14 I, 01.01.1984, p. 4404-4408.

Research output: Contribution to journalArticle

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AB - 125I-labeled protein 4.1a and 4.1b have equal ability to reassociate with inside-out erythrocyte vesicles that were depleted of protein 4.1 in addition to other peripheral membrane proteins. The reassociation of 125I-labeled protein 4.1 to protein 4.1-depleted vesicles at 4°C is salt dependent, pH dependent, and saturable with a K(d) of 42-50 nM and an extrapolated maximal binding capacity of 120-140 μg of protein 4.1 bound per mg of vesicle protein or 60-70 μg of protein 4.1 bound per mg of ghost protein, correlating with the protein 4.1 content in the erythrocyte membrane (6-7% of the total membrane protein). Selective proteolytic cleavage of these vesicles with papain (5 μg/ml at 4°C) eliminates > 60% of the high-affinity binding sites; therefore, we conclude that the interaction of protein 4.1 with the cytoplasmic membrane surface is through a specific high-affinity protein-protein association.

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