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We have determined the amino acid sequence of the N alpha-terminal portion of band 3, the anion transport protein of the human erythrocyte membrane. The material analyzed was a 201-residue, 23,053-Da fragment cleaved from the cytoplasmic end of band 3 by S-cyanylation. The sequence had these notable features. 1) The N alpha-terminal region was extraordinarily acidic, second only to a segment of similar size from the sigma factor of Escherichia coli RNA polymerase. The first 33 residues contained 6 aspartic acid and 12 glutamic acid residues, no basic residue, and a blocked N alpha-amino group. 2) The first 11 residues of the protein had a striking resemblance to the following 11 residues. 3) In contrast to the acidic N alpha-terminal third, the COOH-terminal two-thirds of the 23,053-Da fragment had a predominantly basic character. The highly acidic character of the N alpha-terminal portion of band 3 accounts for the capacity of this part of the protein to bind glycolytic enzymes in a highly electrostatic fashion, presumably through interaction with their cationic substrate-binding sites.
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A G Reddy, and
T L Steck, and
H Kohler
January 1990,
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R K Kaul, and
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February 2003,
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R K Kaul, and
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R K Kaul, and
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R K Kaul, and
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H Kohler
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R K Kaul, and
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R K Kaul, and
S N Murthy, and
A G Reddy, and
T L Steck, and
H Kohler
December 1972,
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R K Kaul, and
S N Murthy, and
A G Reddy, and
T L Steck, and
H Kohler
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R K Kaul, and
S N Murthy, and
A G Reddy, and
T L Steck, and
H Kohler
July 1978,
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R K Kaul, and
S N Murthy, and
A G Reddy, and
T L Steck, and
H Kohler
February 1974,
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