Site-specific modification of hemoglobin by methyl acetyl phosphate.

Abstract:

:Methyl acetyl phosphate, which was originally synthesized as a site-specific reagent for hydroxybutyrate dehydrogenase [R. Kluger and W.-C. Tsui (1980) J. Org. Chem. 45, 2723], also has an affinity for the binding site for 2,3-diphosphoglycerate in hemoglobin. Three residues in or near this cleft between the beta-chains are acetylated by this reagent, i.e., Val-1, Lys-82, and Lys-144. There is no detectable acetylation of any of the amino groups of the alpha-chain. These results indicate the specificity of methyl acetyl phosphate in its reaction with hemoglobin.

journal_name

Arch Biochem Biophys

authors

Ueno H,Pospischil MA,Manning JM,Kluger R

doi

10.1016/0003-9861(86)90648-x

subject

Has Abstract

pub_date

1986-02-01 00:00:00

pages

795-800

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(86)90648-X

journal_volume

244

pub_type

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