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Blue Sepharose chromatography of human alcohol dehydrogenase: evidence for interlocus and interallelic differences in affinity characteristics
Author(s) -
ADINOLFI A.,
HOPKINSON D. A.
Publication year - 1978
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1978.tb00910.x
Subject(s) - isozyme , alcohol dehydrogenase , affinities , locus (genetics) , sepharose , allele , affinity chromatography , alcohol , biology , biochemistry , enzyme , genetics , microbiology and biotechnology , gene
Summary 1. The various isozymes of human alcohol dehydrogenase have been examined by Blue 2. The products (α, β 1 and γ 1 ) of the common alleles a t the three ADH loci (ADH, ADH, and ADH, respectively) were found to show slight, but significant differences in their aflinities for Blue Sepharose. The order of affinity of the homodimeric isozymes was: aa < ylyl < plP1. The heterodimeric isozymes showed intermediate affinities. 3. The products (γ 1 and γ 2 ) of the common alleles (ADH 3 1 and ADH 3 2 respectively) at the ADH, locus showed a pronounced difference in their affinities: the γ 1 γ 1 isozyme was firmly adsorbed by Blue Sepharose, whereas the γ 2 γ 2 isozyme was not adsorbed. The heterodimeric γ 1 γ 2 isozyme was intermediate in its behaviour. 4. The 'usual' and 'atypical' forms of ADH were indistinguishable by Blue Sephasose column chromatography. 5. The 'anodal' form of ADH showed no affinity for Blue Sepharose. We are grateful to the Department of Pathology, Radcliffe Infirmary, Oxford, for tlie adult post‐mortem tissues and to the M.R.C. Tissue Bank at the Royal Marsden Hospital for foetal specimens. We also thank Mrs Caroline Greensted and Miss Geeta Bulsara for their help and the Wellcome Trust for financial support (Wellcome Trust Research Fellowship for Dr A. Adinolfi).