The effect of 2,3-diphosphoglyceric acid on the changes in - interactions in hemoglobin during oxygenation
- PMID: 5135320
Item in Clipboard
The effect of 2,3-diphosphoglyceric acid on the changes in - interactions in hemoglobin during oxygenation
J Biol Chem.
.
Free article
No abstract available
Similar articles
-
Ligand binding and internal equilibria in proteins.Biochemistry. 1972 Feb 29;11(5):864-78. doi: 10.1021/bi00755a028. Biochemistry. 1972. PMID: 5059892 No abstract available.
-
A general model of cooperativity and its application to DPG inhibition of hemoglobin oxygenation.Biochem Biophys Res Commun. 1972 Jul 25;48(2):307-13. doi: 10.1016/s0006-291x(72)80051-2. Biochem Biophys Res Commun. 1972. PMID: 5043184 No abstract available.
-
Stabilizing interactions in hemoglobin.J Biol Chem. 1972 Apr 25;247(8):2345-50. J Biol Chem. 1972. PMID: 5019951 No abstract available.
-
Spin-label studies of cooperative oxygen binding to hemoglobin.Annu Rev Biochem. 1971;40:227-36. doi: 10.1146/annurev.bi.40.070171.001303. Annu Rev Biochem. 1971. PMID: 4330577 Review. No abstract available.
-
[Allosteric effector of hemoglobin, D-2,3-diphosphoglycerate].Tanpakushitsu Kakusan Koso. 1970 Nov;15(13):1328-32. Tanpakushitsu Kakusan Koso. 1970. PMID: 4920708 Review. Japanese. No abstract available.
Cited by
-
Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.Proc Natl Acad Sci U S A. 1976 May;73(5):1581-5. doi: 10.1073/pnas.73.5.1581. Proc Natl Acad Sci U S A. 1976. PMID: 1064027 Free PMC article.
-
Functional nonequivalence of and hemes in human adult hemoglobin.Proc Natl Acad Sci U S A. 1972 Jul;69(7):1707-10. doi: 10.1073/pnas.69.7.1707. Proc Natl Acad Sci U S A. 1972. PMID: 4505648 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
