The Amino Acid Sequences of the α and β Chains of Hemoglobin from the Snake, Liophis Miliaris
作者： M S A Matsuura , K Fushitani , A F Riggs
DOI: 10.1016/S0021-9258(18)83575-X
关键词: Chemistry 、 Bohr effect 、 Globin 、 Amino acid 、 Stereochemistry 、 Heme 、 Cooperativity 、 Alpha chain 、 Liophis miliaris 、 Peptide sequence
摘要: The hemoglobin of Liophis miliaris has unusual properties. is dimeric in the oxy form, and cooperativity O2 binding very low, but both Bohr effect are greatly enhanced presence ATP (Matsuura, M. S. A., Ogo, H., Focesi, Jr. (1987) Comp. Biochem. Physiol. 86A, 683-687). Four unique chains (2 alpha, 2 beta) can be isolated from hemolysate. amino acid sequences one alpha beta chain have been determined an effort to understand functional Comparison with those human Hb shows following. (i) All 7 residues normally conserved globins identical chain: Gly(B6), Phe(CD1), His(E7), Leu(F4), His(F8), Lys(H10), Tyr(HC2), except that distal His(E7) replaced by Gln chain. (ii) heme contact chain, two differences present Met(B13) Leu. (iii) form site for organic phosphates Hb. (iv) major contribute normal Hb, Asp-beta 94, His-beta 146, Val-alpha 1 conserved. (v) at interface two: Glu(G3)----Val Glu(CD2)----Thr; these charged may explain dissociation dimers. (vi) 23 region three: Phe(B14)----Leu, Thr(C3)----Gln Pro(CD2)----Ser. (vii) A total 17 occur interface, 11 6
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