Comparative biochemistry of acid proteinase from animal origins.
Acid proteinases from 17 tissues of 12 animal species were compared with respect to molecular weight, inhibition by pepstatin and activation by tripolyphosphate. Gel filtration of acid proteinases from protochordates and vertebrates showed a common elution profile and three peaks with mol. wts of -20,000, -45,000 and above 150,000 were detected with acid-denatured hemoglobin as substrate at pH 3.6. The main component of vertebrate acid proteinases was identified as cathepsin D. In the invertebrate acid proteinases, the elution profiles through gel filtration were characteristic to the tissues examined, and were not so distinct as those of vertebrates. Through a biochemical survey, the animal acid proteinase was discussed from a comparative point of view.
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D008970:Molecular Weight; D009928:Organ Specificity; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D013045:Species Specificity; D014981:Xenopus
D011480:Protease Inhibitors; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D