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• W1495406918 abstract "Abstract The amino acid compositions of the isolated α and β chains from purified adult cat hemoglobins A and B have been determined. The data indicate that the α chains are similar but the β chains differ by about four substitutions. Amino-terminal analysis has shown the presence of the typical Val-Leu sequence in the cat α chains. However, the two β chains differ at their amino terminals. NH2-terminal glycine is found in the A-β and a serine with a blocked α-NH2 group occurs in this position in the B-β chain. The amino-terminal tryptic peptides of both β chains have been isolated and their sequences partially characterized. The effects of 2,3-diphosphoglycerate and ATP on the oxygen saturation curves of isolated cat hemoglobins A and B (HbA and HbB) have been investigated. Cat HbA, with free β chain NH2 termini, is sensitive to 2,3-diphosphoglycerate and ATP, whereas cat HbB, with blocked β chain NH2 termini, is insensitive to these effector molecules. The oxygen affinities of the hemolysates containing mixtures of HbA and HbB are changed by 2,3-diphosphoglycerate or ATP in proportion to the ratio of HbA to HbB in the hemolysate. The work provides support for a role of the NH2 terminus of the β chain in the control of oxygen binding in hemoglobin." @default.
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• W1495406918 date "1971-07-01" @default.
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• W1495406918 title "β Chain Amino Termini of the Cat Hemoglobins and the Response to 2,3-Diphosphoglycerate and Adenosine Triphosphate" @default.
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• W1495406918 doi "https://doi.org/10.1016/s0021-9258(18)62035-6" @default.
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