Band 3 protein of the red cell membrane of the llama: Crosslinking and cleavage of the cytoplasmic domain

Jena K. Khodadad, Ronald S Weinstein

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Comparative studies were done on the cytoplasmic domain of the band 3 protein in the red cell membranes of the the human and the llama. Two approaches were used: crosslinking with o-phenanthroline/CuSO4, and cleavage with 2-nitro-5-thiocyano-benzoate. o-Phenanthroline/CuSO4 crosslinks the band 3 polypeptide chains in the human; in contrast band 3 in the llama is minimally crosslinked by this agent. 2-Nitro-5-thiocyano-benzoate cleaves band 3 in the human into a 23,000-dalton fragment; a similar fragment is not generated from the llama band 3. These studies show that the cysteine residue located 23,000 daltons from the N-terminus of band 3 in the human involved in these reactions is unavailable for crosslinking and cleavage in the llama. Species differences in the cytoplasmic domain of band 3 may contribute to the unusual resistance of llama red cells to osmotic, chemical and physically-induced deformation.

Original languageEnglish (US)
Pages (from-to)493-499
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume130
Issue number1
DOIs
StatePublished - Jul 16 1985
Externally publishedYes

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Erythrocyte Anion Exchange Protein 1
New World Camelids
Benzoates
Cell membranes
Crosslinking
Cell Membrane
Cysteine
Cells
Peptides
1,10-phenanthroline

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Band 3 protein of the red cell membrane of the llama : Crosslinking and cleavage of the cytoplasmic domain. / Khodadad, Jena K.; Weinstein, Ronald S.

In: Biochemical and Biophysical Research Communications, Vol. 130, No. 1, 16.07.1985, p. 493-499.

Research output: Contribution to journalArticle

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