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© 1993 Medical Council on Alcohol

research-article

INFLUENCE OF PYRUVATE, THREONINE AND PHOSPHOETHANOLAMINE ON ACTIVITIES OF SOME ACETALDEHYDE-PRODUCING ENZYMES

D. GERASHCHENKO, B. GORENSHTEIN, T. PYZHIK and Yu. OSTROVSKY{maltese cross}

Institute of Biochemistry, Academy of Sciences 230009 Grodno, BLK-50, Republic of Belarus, C.I.S.

Received 20 July 1992; first review notified 1 February 1993; accepted 5 February 1993

Threonine (50 mg/100 g, i.p.) leads to increased hepatic threonine aldolase activity in rats, although endogenous ethanol concentrations remain stable After pyruvate administration (50 mg/100 g, i.p.), endogenous blood ethanol levels are raised within 30 min, but return to normal at 60 min. The activity of threonine aldolase is decreased in the liver, whereas phosphoethanolamine lyase and pyruvate dehydrogenase activities remain unchanged. Phosphoethanolamine administration (23 mg/100 g, i.p.) did not change the endogenous ethanol concentration or pyruvate dehydrogenase, threonine aldolase and phosphoethanolaminc lyase activities. Pyruvate appears to be a better precursor of acetaldehyde than threonine or phosphoethanolamine.


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