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 Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Ueno H,Pospischil MA,Manning JM,Kluger Rdoi
10.1016/0003-9861(86)90648-xsubject
Has Abstractpub_date
1986-02-01 00:00:00pages
795-800issue
2eissn
0003-9861issn
1096-0384pii
0003-9861(86)90648-Xjournal_volume
244pub_type
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journal_title:Archives of biochemistry and biophysics
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