Peromyscus alcohol dehydrogenase: Lack of cross-reacting material in enzyme-negative animals

Abstract

Two forms of alcohol dehydrogenase (ADH), coded by allelic genes, have been purified to homogeneity from Peromyscus. Monospecific antisera to the purified enzymes have been raised in rabbits. These antisera fail to detect cross-reacting material in the liver of ADH-negative animals on Ouchterlony plates. Immunotitration of anti-ADH antiserum with ADH in liver extracts from Adh ^S/Adh ^S and Adh ^S/Adh ^N animals results in identical equivalence points, again suggesting the absence of cross-reacting material coded by the Adh ^N allele. Over a wide range of anti-ADH antiserum dilutions, radiolabeled protein was not immunoprecipitable from liver extracts of Adh ^N/Adh ^N animals. These immunochemical tests, in conjunction with previous studies, suggest that the Adh ^N allele in Peromyscus does not produce inactive polypeptide in normal levels that bears immunological determinants similar to those of the fast and slow ADH isozymes.