Misincorporation of alkylated amino acids into hemoglobin--a possible source of background alkylations.
Misincorporation of 2-hydroxyethylated amino acids into hemoglobin during de novo synthesis was studied by injecting mice with radiolabelled N-(2-hydroxyethyl)valine, S-(2-hydroxyethyl)cystine or N tau-(2-hydroxyethyl)histidine. The results showed that S-(2-hydroxyethyl)cysteine and N tau-(2-hydroxyethyl)histidine were misincorporated, whereas N-(2-hydroxyethyl)valine was not. Monitoring of in vivo doses of hydroxyethylating agents by determination of N-(2-hydroxyethyl)valine was free of the disturbing influence of such misincorporation.
D000478:Alkylation; D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D005914:Globins / Q000096:biosynthesis / Q000302:isolation & purification; D006454:Hemoglobins / Q000096:biosynthesis*; D008297:Male; D051379:Mice; D008808:Mice, Inbred CBA; D013329:Structure-Activity Relationship
D000596:Amino Acids; D006454:Hemoglobins; D005914:Globins