TY - JOUR
T1 - Prosimian hemoglobins I. The primary structure of the βglobin chain of lemur catta
AU - Coppenhaver, Dorian H.
AU - Dixon, James D.
AU - Duffy, Lawrence K.
N1 - Funding Information:
ACKNOWLEDGMENTS We thank Mr. Horace Kelsoe for expert technical assistance. Supported in part by a grant from the American Philosophical Society REFERENCES Holmquist, R., Jukes, T.H., Goodman, M., and Moore, G.W., Biol., K z 3 9 - 7 4 , 1976.
PY - 1983
Y1 - 1983
N2 - The primary structure of the β chain from the hemoglobin of a prosimian primate, Lemur catta, has been determined by automated Edman degradation of intact polypeptide chain and fragments produced by tryptic, cyanogen bromide and acid cleavage, and by homology with the sequence of Lemur fulvus. The sequence presented here differs from the human βglobin sequence at 26 sites. This is the same degree of divergence previously reported for the βglobin chain of Lemur fulvus. The sequences of the two congeneric lemuroid βglobin chains are surprisingly divergent, differing at 18 sites. Of the 26 positions where L. catta differs from Homo sapiens, 7 are at positions with defined function. Of these 7 positions, 4 (2-Phe, 54-Ile, 94-Val, 112-Ile) are unique to L. catta among the primate βglobin chains of established sequence. Residue 112-Ile is consistent with the prediction of Beard and Goodman (19) of an isoleucyl residue in this position in the ancestral primate βglobin chain.
AB - The primary structure of the β chain from the hemoglobin of a prosimian primate, Lemur catta, has been determined by automated Edman degradation of intact polypeptide chain and fragments produced by tryptic, cyanogen bromide and acid cleavage, and by homology with the sequence of Lemur fulvus. The sequence presented here differs from the human βglobin sequence at 26 sites. This is the same degree of divergence previously reported for the βglobin chain of Lemur fulvus. The sequences of the two congeneric lemuroid βglobin chains are surprisingly divergent, differing at 18 sites. Of the 26 positions where L. catta differs from Homo sapiens, 7 are at positions with defined function. Of these 7 positions, 4 (2-Phe, 54-Ile, 94-Val, 112-Ile) are unique to L. catta among the primate βglobin chains of established sequence. Residue 112-Ile is consistent with the prediction of Beard and Goodman (19) of an isoleucyl residue in this position in the ancestral primate βglobin chain.
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U2 - 10.3109/03630268309038398
DO - 10.3109/03630268309038398
M3 - Article
C2 - 6841124
AN - SCOPUS:0020623776
SN - 0363-0269
VL - 7
SP - 1
EP - 14
JO - Hemoglobin
JF - Hemoglobin
IS - 1
ER -