TY - JOUR
T1 - Band 3 protein of the red cell membrane of the llama
T2 - Crosslinking and cleavage of the cytoplasmic domain
AU - Khodadad, Jena K.
AU - Weinstein, Ronald S.
PY - 1985/7/16
Y1 - 1985/7/16
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(85)90444-9
DO - 10.1016/0006-291X(85)90444-9
M3 - Article
C2 - 4026842
AN - SCOPUS:0022368585
SN - 0006-291X
VL - 130
SP - 493
EP - 499
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -