Alcohol Dehydrogenase Isozymes in Baboons: Tissue Distribution, Catalytic Properties, and Variant Phenotypes in Liver, Kidney, Stomach, and Testis

Publisher Website
Google Scholar
Abstract
Isoelectric focusing and cellulose acetate electrophoresis were used to examine the multiplicity, tissue distribution, and variability of alcohol dehydrogenase (AOH) among baboons, a primate species used as a model for research on alcohol metabolism and alcohol‐induced liver pathology. Five major AOH isozymes were resolved and distinguished on the basis of their isoelectric points, tissue distributions, relative activities with alcohol substrates, and sensitivities to inhibition with 4‐methyt pyrazote. ADH‐1 and ADH‐2 exhibited class I kinetic properties and were observed in high activity in kidney and liver extracts, respectively. ADH‐3 showed class II kinetic properties, exhibiting high activity in stomach extracts, and was widely distributed in extracts of other baboon tissues, including kidney, esophagus, heart, testis, brain, and male sex accessory tissues. ADH‐4 also showed class II ADH properties but was found only in liver (similar to human “x‐ADH”). ADH‐5 exhibited class III AOH kinetic properties, being inactive with ethanol up to 0.5 M (similar to human “x‐ADH”) and was distributed widely in baboon tissue extracts. Major activity variation was observed for liver ADH‐4 between different animals. An electrophoretic variant for ADH‐3 was observed for the enzyme in stomach, kidney, and testis extracts, and activity variation existed for this isozyme in kidney extracts. It is apparent that baboon ADH shares a number of features with the human ADH phenotype; however, several species‐specific differences were observed, particularly for the liver and kidney class I isozymes and for stomach ADH.

This publication has 50 references indexed in Scilit: