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Inhibition of the gelation of extracellular and intracellular hemoglobin S by selective acetylation with methyl acetyl phosphate.
Biochemistry. 1987 Jun 02; 26(11):3125-9.B

Abstract

Methyl acetyl phosphate binds to the 2,3-diphosphoglycerate (2,3-DPG) binding site of hemoglobin and selectively acetylates three amino groups at or near that site. The subsequent binding of 2,3-DPG is thus impeded. When intact sickle cells are exposed to methyl acetyl phosphate, their abnormally high density under anaerobic conditions is reduced to the density range of oxygenated, nonsickling erythrocytes. This change is probably due to a combination of direct and indirect effects induced by the specific acetylation. The direct effect is on the solubility of deoxyhemoglobin S, which is increased from 17 g/dL for unmodified hemoglobin S to 22 g/dL for acetylated hemoglobin S at pH 6.8. Acetylated hemoglobin S does not gel at pH 7.4, up to a concentration of 32 g/dL. The indirect effect could be due to the decreased binding of 2,3-DPG to deoxyhemoglobin S within the sickle erythrocyte, thus hindering the conversion of oxyhemoglobin S to the gelling form, deoxyhemoglobin S.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

3607016

Citation

Ueno, H, et al. "Inhibition of the Gelation of Extracellular and Intracellular Hemoglobin S By Selective Acetylation With Methyl Acetyl Phosphate." Biochemistry, vol. 26, no. 11, 1987, pp. 3125-9.
Ueno H, Benjamin LJ, Pospischil MA, et al. Inhibition of the gelation of extracellular and intracellular hemoglobin S by selective acetylation with methyl acetyl phosphate. Biochemistry. 1987;26(11):3125-9.
Ueno, H., Benjamin, L. J., Pospischil, M. A., & Manning, J. M. (1987). Inhibition of the gelation of extracellular and intracellular hemoglobin S by selective acetylation with methyl acetyl phosphate. Biochemistry, 26(11), 3125-9.
Ueno H, et al. Inhibition of the Gelation of Extracellular and Intracellular Hemoglobin S By Selective Acetylation With Methyl Acetyl Phosphate. Biochemistry. 1987 Jun 2;26(11):3125-9. PubMed PMID: 3607016.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inhibition of the gelation of extracellular and intracellular hemoglobin S by selective acetylation with methyl acetyl phosphate. AU - Ueno,H, AU - Benjamin,L J, AU - Pospischil,M A, AU - Manning,J M, PY - 1987/6/2/pubmed PY - 1987/6/2/medline PY - 1987/6/2/entrez SP - 3125 EP - 9 JF - Biochemistry JO - Biochemistry VL - 26 IS - 11 N2 - Methyl acetyl phosphate binds to the 2,3-diphosphoglycerate (2,3-DPG) binding site of hemoglobin and selectively acetylates three amino groups at or near that site. The subsequent binding of 2,3-DPG is thus impeded. When intact sickle cells are exposed to methyl acetyl phosphate, their abnormally high density under anaerobic conditions is reduced to the density range of oxygenated, nonsickling erythrocytes. This change is probably due to a combination of direct and indirect effects induced by the specific acetylation. The direct effect is on the solubility of deoxyhemoglobin S, which is increased from 17 g/dL for unmodified hemoglobin S to 22 g/dL for acetylated hemoglobin S at pH 6.8. Acetylated hemoglobin S does not gel at pH 7.4, up to a concentration of 32 g/dL. The indirect effect could be due to the decreased binding of 2,3-DPG to deoxyhemoglobin S within the sickle erythrocyte, thus hindering the conversion of oxyhemoglobin S to the gelling form, deoxyhemoglobin S. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/3607016/Inhibition_of_the_gelation_of_extracellular_and_intracellular_hemoglobin_S_by_selective_acetylation_with_methyl_acetyl_phosphate_ L2 - https://www.lens.org/lens/search/patent/list?q=citation_id:3607016 DB - PRIME DP - Unbound Medicine ER -