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Molecular Evolution of Prosimian Hemoglobins

✍ Scribed by LAWRENCE K. DUFFY; DORIAN H. COPPENHAVER


Book ID
118721351
Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
147 KB
Volume
435
Category
Article
ISSN
0890-6564

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πŸ“œ SIMILAR VOLUMES


Prosimian hemoglobins: IV. The structura
✍ Lawrence K. Duffy; Margaret M. Ehrhardt; John Buettner-Janusch; Dorian H. Coppen πŸ“‚ Article πŸ“… 1987 πŸ› John Wiley and Sons 🌐 English βš– 405 KB

The ring-tailed lemur, Lemur catta, shows a two-component hemoglobin phenotype after alkaline electrophoresis. A difference in the amino acid sequence of the isolated a-globins was observed at position 15 (a I-Gly, a II-Lys) and can account for the electrophoretic pattern of two hemoglobin component

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Evolution of cooperativity in hemoglobin
✍ Kitto, G. Barrie; Thomas, P. W.; Hackert, M. L. πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 437 KB

While vertebrate hemoglobins typically are tetrameric and show highly regulated and cooperative ligand binding, little is known of the evolution of these properties. We are studying the structural and functional properties of the hemoglobins from Caudina arenicola, an echinoderm. The echinoderms are