TY - JOUR
T1 - Evidence for the formation of multiple types of acetaldehyde-haemoglobin adducts
AU - Gross, Myron D
AU - Hays, Rebecca
AU - Gapstur, Susan M.
AU - Chaussee, Mike
AU - Potter, John D.
PY - 1994/1
Y1 - 1994/1
N2 - Acetaldehyde readily reacted with red blood cells and isolated haemoglobin to form adducts. We examined acetaldehyde-haemoglobin reaction products, isolated from red blood cells incubated with acetaldehyde (AcH), for the presence of stable peptide-specific acetaldehyde adducts. Red blood cell incubations were with 20, 50, and 200 mM acetaldehyde for 3, 24 and 48 hr. Peptide-specific [14C]acetaldehyde modifications of Hb from each incubation were identified by tiyptic peptide mapping procedures. Nine peptides had modifications and six were found in incubations with 20 mM acetaldehyde. Two of the peptides were acetaldehyde modifications of the Hb α- and β-chain N-termini. Stability studies indicated that the remaining seven [14C]AcH-modified peptides did not result, as can occur under certain conditions, from the transfer of AcH on the N-termini of Hb to N-termini formed after trypsin digestion. An analysis of the relative amounts of [14C]AcH-peptide adducts indicated that at least two of the seven peptides had reactivities for AcH different than the N-termini of Hb; that is, at least two modified peptides differ from imidazolidine-type adducts formed on the N-termini. The presence of multiple modifications with different sensitivities for AcH adduct formation may be useful in developing markers of alcohol consumption.
AB - Acetaldehyde readily reacted with red blood cells and isolated haemoglobin to form adducts. We examined acetaldehyde-haemoglobin reaction products, isolated from red blood cells incubated with acetaldehyde (AcH), for the presence of stable peptide-specific acetaldehyde adducts. Red blood cell incubations were with 20, 50, and 200 mM acetaldehyde for 3, 24 and 48 hr. Peptide-specific [14C]acetaldehyde modifications of Hb from each incubation were identified by tiyptic peptide mapping procedures. Nine peptides had modifications and six were found in incubations with 20 mM acetaldehyde. Two of the peptides were acetaldehyde modifications of the Hb α- and β-chain N-termini. Stability studies indicated that the remaining seven [14C]AcH-modified peptides did not result, as can occur under certain conditions, from the transfer of AcH on the N-termini of Hb to N-termini formed after trypsin digestion. An analysis of the relative amounts of [14C]AcH-peptide adducts indicated that at least two of the seven peptides had reactivities for AcH different than the N-termini of Hb; that is, at least two modified peptides differ from imidazolidine-type adducts formed on the N-termini. The presence of multiple modifications with different sensitivities for AcH adduct formation may be useful in developing markers of alcohol consumption.
UR - http://www.scopus.com/inward/record.url?scp=0028205655&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028205655&partnerID=8YFLogxK
M3 - Article
C2 - 8003114
AN - SCOPUS:0028205655
SN - 0735-0414
VL - 29
SP - 31
EP - 41
JO - Alcohol and Alcoholism
JF - Alcohol and Alcoholism
IS - 1
ER -