Primary structure of the marmoset (Saguinus fuscicollis) hemoglobin. I. Use of tryptic maleylated peptides in the solubilization and sequence elucidation of the ?- and ?-chains

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Abstract
The primary structure of adult marmoset hemoglobin has been determined. The α- and β-chains of HbA were separated on a CM23 column in 8 M urea using a sodium phosphate gradient. Tryptic digests of the α- and β-chains were fractionated on a Dowex 50W-X2 column using a pH and pyridine acetate gradient. Large peptide fragments were obtained by the cyanogen bromide cleavage of the α- and β-chains, as well as by tryptic digestion of the maleylated α- and β-chains. The sequence was derived from the amino acid compositions and sequences of the individual tryptic peptide, automated sequence determination of intact α- and β-chains, as well as automated sequence determination of cyanogen bromide fragments and tryptic maleylated peptides derived from the α- and β-chains. The complete structure of marmoset adult hemoglobin is closely homologous to that of other primate hemoglobins. The sequence of the marmoset α-chain differs from the α-chain of human HbA at positions 8, 19, 23, 68, and 116. The β-chain from marmoset HbA differs from the β-chain of human HbA at positions 5, 13, 21, 50, 87, and 125.