Summary
The trypsin of three species of frogs (Rana esculenta, R. ridibunda, R. temporaria), of the tadpoles ofR. temporaria, of two species of fish (Salmo trutta, Tinca tinca) and of the lizard,Lacerta muralis, were separated by agar gel electrophoresis, eluted and partly characterized.
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1.
Three isozymes were found in the frogs, one in the tadpole, three in the trout, four in the tench and two in the lizard. The isozyme pattern of the frogs is remarkably constant whereas those of the fishes and the lizard appear to be more variable under the influence of environmental factors. The single trypsin of the tadpole does not resemble any of the adult trypsins ofR. temporaria.
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2.
The affinity for DL-BAPA of all isozymes of trypsin examined varies by a factor of approximately 20 (Table 1), but in most cases there is little dependence ofK m (app) on temperature and pH in the physiological range.
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3.
In amphibians and reptiles substrate affinity (expressed asK m (app)) and stability (expressed as the half life at pH 8.2 and 30° C) are negatively correlated, whereas the isozymes of fishes (with the exception of T2 of the tench), despite their relatively high affinity, are stable at a pH of 8.2.
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Hofer, R., Schiestl, W., Gattringer, A. et al. Trypsin isozymes of some ectothermic vertebrates. J Comp Physiol B 101, 111–119 (1975). https://doi.org/10.1007/BF00694152
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DOI: https://doi.org/10.1007/BF00694152