Amino acid compositions of the tryptic peptides comprising the β-hemoglobin chain of Macaca nemestrina
✍ Scribed by Peter E. Nute; H. A. Pataryas
- Publisher
- John Wiley and Sons
- Year
- 1974
- Tongue
- English
- Weight
- 524 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0002-9483
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✦ Synopsis
Abstract
The tryptic peptides comprising the aminoethylated β‐hemoglobin chain of Macaca nemestrina were isolated by paper electrophoresis and chromatography. The results of stains for specific amino acids, comparison of peptide maps with those produced by aminoethlated β chains from human hemoglobin A, and amino acid analyses of all peptides in the macaque β chain support the conclusion that the primary structure of the β chain of M. nemestrina is identical to that of the corresponding chains of M. fuscata fuscata and M. fascicularis. The apparent evolutionary conservatism of macaque β chains is discussed in relation to the wide degree of structural variation previously observed among the α‐hemoglobin chains of several species of Macaca.
📜 SIMILAR VOLUMES
The primary structure of adult marmoset hemoglobin has been determined. The alpha- and beta-chains of HbA were separated on a CM23 column in 8 M urea using a sodium phosphate gradient. Tryptic digest of the alpha- and beta-chains were fractionated on a Dowex 50W-X2 column using a pH and pyridine ace