Tissue- and species-specificity of alkaline phosphatase in marine animals
| Autor: | Hiroki Abe, Sachiko Gotoh |
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| Rok vydání: | 1981 |
| Předmět: | |
| Zdroj: | NIPPON SUISAN GAKKAISHI. 47:267-273 |
| ISSN: | 1349-998X 0021-5392 |
| DOI: | 10.2331/suisan.47.267 |
| Popis: | Alkaline phosphatase (EC 3.1.3.1) from various tissues of skipjack, Katsuwonus pelamis, and also from hepatic tissues of several marine animals were examined for some enzymatic properties. The total activity of the enzymes from skipjack tissues was high in the pyloric caecum, kidney, and liver, but low in the ordinary and cardiac muscles, and bone. The enzyme activeity of fish livers was higher than that of invertebrate hepatopancreas. The optimal pH values of skipjack enzymes significantly differed from the kind of tissues, rangin from 7.3 to 10.2 The hepatic enzymes from most marine animals, however, showed similar optimal values around pH 10, except those from skipjack (pH 8.8) and prawn (pH 8.4). Michaelis constants of the enzymes were found between 0.02 and 0.1 mM against p-nitrophenyl phosphate. The inhibitory effects of several effectors, such as p-chloromercuribenzoate, L-tryptophan, and L-phenylalanine, on the enzymes depended on the tissues and on the species. The skipjack enzymes seemed to be divided into two groups as to their heat stability. On cellulose acetate electrophoresis, the skipjack enzymes showed different isoenzyme patterns depending on the tissues. It was concluded from the above data that the tissue-specificity of alkaline phosphatase is much higher than its species-specificity. |
| Databáze: | OpenAIRE |
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