The Identification and Partial Characterization of Acetaldehyde Adducts of Hemoglobin Occurring in Vivo: A Possible Marker of Alcohol Consumption

Myron D Gross, Susan M. Gapstur, John D Belcher, Gale Scanlan, John D. Potter

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Chromatographic, peptide mapping and mass spectrometric analysis were used to examine hemoglobin (Hb) from heavy drinkers and abstainers for alcohol consumption‐related modifications. Heavy drinker and abstainer hemoglobin samples contained similar amounts of glycosylated Hb and significantly different (p < 0.05) amounts of “fast” hemoglobin. The presence of higher amounts of “fast” Hb in heavy drinker relative to abstainer samples suggested the presence of alcohol‐consumption related modifications. To further examine Hb for modifications, tryptic peptides of the “fast” hemoglobin HbA1c were isolated and analyzed by plasma desorption mass spectrometry (PDMS). [14Clacetaldehyde (AcH)‐Hb was synthesized in vivo for use as standard. Specific peptides were chosen based on co‐migration with radiolabeled peptides from tryptic digest of the [14C]acetaldehyde‐Hb. The masses obtained by PDMS for two heavy drinker peptides were identical to two radiolabeled peptides; the two pairs of peptides co‐migrated on HPLC. A comparison of the observed mass for the peptides with the theoretical masses for acetaldehyde‐modified Hb peptides suggested that the peptides were AcH‐modified alpha and beta chain N‐termini of Hb. The modified peptides were found in five of six heavy drinker samples. This is the first description of site‐specific AcH‐Hb adducts occurring in vivo. The routine detection of such adducts has potential for characterizing usual alcohol intake.

Original languageEnglish (US)
Pages (from-to)1093-1103
Number of pages11
JournalAlcoholism: Clinical and Experimental Research
Volume16
Issue number6
DOIs
StatePublished - Dec 1992

Keywords

  • AcH‐Hb adducts
  • PDMS
  • in vivo

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