By examining the electrophoretic patterns of some fish serum protein obtained under almost the same condition, the author ascertained the following fact that the specificity, in quantity as well in quality, of the serum protein composition was more or less conspicuous corresponding to their classification of species or to the habitual environment.
(1) In cases of fresh-water teleosts such as,
Cyprinus carpio, and
Carassius auratus, component I which might correspond, in its mobility, to the human serum albumin is most rich amoung the serum proteins, while in cases of marine teleosts,
Chrysophrys major, Trachurus japonicus, Decapterus muroadsi, Coryphaena hippurus, Scomber tapeinocephalus, Thunnus thynnus, the presence of the component-f, with the higher mobility than albumin, is apparent, in addition to the component I . The component-f is apt to appear most abundantly among the serum proteins.
On the other hand. in the serum proteins of the marine elasmobranchs,
Squalus mitsukurii, Mustelus griseus, there is no detectable amount of the component I to say nothing of the compo-nent-f, but the component II and IV + IV', which correspond maybe to the human serum globulins, are contained in comparatively large amounts.
(2) Generally, in cases of teleosts, the concentration of the component, which corresponds to the ϒ-globulin of human serum, is far less than the control serum (human and rabbit), but in cases of the shark serum the the extraordinarily high concentration of this fraction is found.
(3) The albumin/globulin ratio of the serum protein in cases of marine teleosts is higher than that of the control serum. By using the salt fractionation method it was ascertained that the mackerel serum protein was composed mostly of the albumin fraction, while in the shark's contra-rily, most of them were composed of globulin fractions.
(4) The use of the refractometry as the measuring means of shark serum protein cencen-tration was proved to be inadequate.
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