COMPLETE AMINO-ACID SEQUENCE OF THE GAMMA-CHAIN FROM THE MAJOR FETAL HEMOGLOBIN OF THE PIG-TAILED MACAQUE, MACACA-NEMESTRINA

The complete primary structure of the γ chain of the major fetal hemoglobin from the pig-tailed macaque, Macaca nemestrina, was obtained by the automated sequencing of fragments produced by three nonenzymatic cleavage reactions. About two-thirds of the sequence was established from the amino terminus of the intact chain and two of the three fragments produced by cleavage at methionyl residues by cyanogen bromide. Acid cleavage at the single aspartyl-prolyl linkage and cleavage at tryptophanyl residues in intact chains yielded the two fragments necessary to complete the sequence. This γ chain, the first from a non-human primate to be sequenced, differs from the human Gγ and aγ chains at but 4 and 5 positions, respectively. All substitutions are conservative and unlikely to produce alterations in the oxygen-binding properties of the tetrameric fetal hemoglobin. Consideration of the data presented herein, together with published observations made on portions of other primate γ chains, provides some insight into the evolutionary history of the multiple γ-globin chains observed in several anthropoid primates. © 1979, American Chemical Society. All rights reserved.