Adenylate Kinase in Human Tissues

Abstract

Abstract The organ specificity of human adenylate kinase isoenzymes was established among adenylate kinase isoenzymes of different tissue origins by differences in the degree of inhibitions by sulfhydryl reagents; by differences in isoelectric points; by differences of enzyme distribution patterns; and in some instances by differences in molecular weights. The organ specificity of the adenylate kinase isoenzymes obtained also in dog, rat, guinea pig, rooster, fish, and cow. At least six different tissue-specific adenylate kinase isoenzymes were evident in man and several other animal species. The organ specificity of the adenylate kinase was further supported by serological studies. An antiserum against rabbit muscle adenylate kinase inhibited extensively the adenylate kinase activities of the skeletal muscles from all of the species tested, but inhibited slightly or did not inhibit the adenylate kinase activities from the liver or kidneys of these species. The adenylate kinase activities from other tissues showed degrees of inhibition by the antiserum intermediate to liver or kidney adenylate kinase and skeletal muscle adenylate kinase.