The Japanese Journal of Veterinary Science
Online ISSN : 1881-1442
Print ISSN : 0021-5295
ISSN-L : 0021-5295
STUDIES ON THE FRACTIONATION OF FOWL BLOOD PLASMA PROTEIN WITH ETHANOL
Kazuhiko YAMADA
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1971 Volume 33 Issue 6 Pages 301-314

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Abstract
So far as the author is aware, no methods have been established as yet for systematic separation of the fowl blood plasma protein. Under these circumstances, the author tried to fractionate the plasma protein by means of the 6th and 9th methods given by COHN and ONCLEY, and discussed the question whether COHN and ONCLEY's methods were useful for the fractionation of fowl blood plasma protein. The results obtained are summarized as follows. 1. Protein components of individual fractions which are evident on inspection of electrophoretic patterns obtained by electrophoresis on cellulose acetate membrane. a. Fractionation of blood plasma into five major fractions by the 6th method of COHN. [table] b. Fractionation by the 9th method of ONCLEY. [table] 2. Final concentration of ethanol and pH range which are desirable for fractional precipitation of the fowl plasma proteins. [table] In view of the experimental evidence collected for this report, it is possible to state definitely as follows. The fact that the successive fractional precipitation of blood plasma at a controlled pH and a controlled ethanol concentration gave rise to a fairly purified precipitation offers a helpful suggestion that some proper protein components may be selected from the fowl blood plasma. Namely, the 6th method of COHN is effective mainly for the separation of albumin (V) and fibrinogen (I). Furthermore, the 9th method introduced by ONCLEY is useful for the separation of the greater part of the gamma-globulins (II-I, 2, and 3) and the subfractions of albumin and alpha-, beta-, and gamma-globulins (IV-5, 6, 7, and 8). 3. Speciality of subfractions obtained from fraction IV-4. Especially in fraction IV-5, cholesterol existed in abundance and was mainly composed of betalipoproteins. The rest of the fractions were poor in cholesterol. Fracitons IV-5 and IV-6 were rich in glucoprotein. Traces of glucoprotein were present in the remaining fractions. An intense absorption at a wavelength of 414mμ was characteristic of fractions IV-6 and IV-7. From this absorbancy, it appears that the fractions may have an absorptive action upon beta 1-metal combining protein or heme protein.
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