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Abstract
Hemoglobin A1b is a minor hemoglobin component from human hemolysate (less than 0.5% of total hemoglobin) whose structure has never been established. It was purified and studied by mass spectrometry. Electrospray ionization of its abnormal beta-chain indicated a 70-Da mass increase. Separation of the trytic digest by reversed-phase liquid chromatography revealed an abnormal beta T1 peptide. Cesium ion bombardment ionization produced a protonated molecular ion at m/z 1022.516, showing an additional C3H2O2 residue to normal beta T1. The amino acid sequences of both abnormal and normal beta T1 peptides were found identical by comparison of their collision activation spectra. Time course hydrolysis of abnormal beta T1 indicated a rapid loss of the modifying group, leading to normal beta T1. At least, mild treatment with acidic methanol showed an additional methylated site, comparatively with normal beta T1. All these results are consistent with a ketimine-linked pyruvic acid at the amino end of the beta-chain of hemoglobin.
Highlights
Hemoglobin AI, is a minor hemoglobincomponent from human hemolysatewhose structure has never been established
In 1959, Clegg and Schroeder (3), utilizing Amberlite IRC-50 chromatography demonstrated the presence of five minor components and named them hemoglobins AI, Alb, A, Ald, and Ale according to their elution order
Preliminary results have been already presented at the 2nd International Symposium on Applied Mass Spectrometry in the Health Sciences (Barcelona, April 17-20, 1990)
Summary
Hemoglobin AI,, is a minor hemoglobincomponent from human hemolysate (less than 0.5%of total hemoglobin)whose structure has never been established. Time course hydrolysis of abnormal BT1 indicated a rapid loss of the modifying group, leading to normal BT1.At least, mild treatment with acidic methanol showed an additional methylated site, comparatively with normal BT1. All these results are consistent with a ketiminelinked pyruvic acid at the amino end of the &chain of hemoglobin.
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