Abstract
In recent years, some trials for separating the plasma protein components have beenput in practice by the author33=3) to explain the behavior of transaminases in fowl bloodplasma and their physicochemical properties.As a result, it was pointed out that several components obtained by subfractionationof albumin37) and beta-globulins36) were regarded satisfactorily as carriers of reverse (R)-aspartate aminotransferase (GOT), R-alanine aminotransferase (GPT), and reversibleGPT. Several physicochemical determinations laave already been performed to clarifythe properties of these components36?37).On the contrary, it is known that the fairly effective purification of ant active material?on1y for forward (F)-GOT substrate was accomplished as fraction IV-73?35). Moreover, aprotein component with an active fragment of F-GOT has frequently been found in acertain globulin group3?35). Notwithstanding, that fraction has not yet been subjectedto a highly effective purification, because the problem of how to separate and purify itremains unsettled. In order to obtain a basic solution for this problem, it is necessary to?devise a method for systematic separation of blood plasma globulins.The present report deals with a method developed and introduced into practical, application by the author.The results of experiments with this method are summarized as follows.I. On the basis of the relations among several quantities listed in some tables, acomponent distinguishable by disc electrophoresis that had migrated to position 5-b wasobtained by subfractionation from the original fraction, IV-4, as fraction IV-4(d). It wasfound to be F-GOT. Moreover, one of the R-GPT samples existed among the conjugatedprotein components with the relative position, 6-a to b. This conjugated component wasobtained from the original fraction, IV-l, as fraction IV-1(f).2. These components were found to be globulin with the same relative position asgamma.-globulins by the use of cellulose acetate electrophoresis"9?33). This result was thesame as obtained from components 4-b and c36).These data lend support to the conclusion that a few gammax-globulins are constantlypresent in fowl blood plasma and that their fractionation can be carried out. It is im-portant to test tavailable are carried only by the GOT group. It became evident that components 5-band 4-c were derixzed from the reaction of transamination with F-GOT and R-GOT, respectively.If relations among several isozymes of R-GPT or CRT-ase36?37) are examined, it willbe noted that the carriers of these isozymes are evenly distributed among several compo-nents obtained from albumin and globulins. This does not necessarily mean, however, all the isozymes show the same distribution.As mentioned above, on certain reverse transaminases, especially those of the R-GPTgroup, these isozymes seem to have an important action. This considration is ttseful, especially when the physiological function of the GPT group is studied.For this reason, it is interesting to obtain more detailed information on this aspectfrom future investigation.
