Journal of the Japan Veterinary Medical Association
Online ISSN : 2186-0211
Print ISSN : 0446-6454
ISSN-L : 0446-6454
Cellulose Acetate Membrane Electrophoretic Patterns of Bovine Serum Proteins
HIROFUMI SENDA
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1992 Volume 45 Issue 3 Pages 159-165

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Abstract

Electrophoretic Patterns of bovine serum proteins on cellulose acetate membrane (using SEPARAX) were classified into four groups consisting of 14 types in 371 cattle of 33 farms based on mobility and amount of β-and γ-globulin fraction.
Typing of the electrophoretic patterns was made in groups of (1) healthy cattle, (2) cattle in highly infected areas withFasciolasp. and (3) cattle on farms Prevalent with various diseases. In the healthy cattle group, small peaks appeared in the central areas of γ-globulin fraction, many of which were classified into types A to D of group I. In the second group, most of the electrophoretic patterns belonged to types G, H and I of group II, in which peaks appered in the first half areas (anode side) of γ-globulin fraction. The cattle on N farm in this area had been treated periodically with vermifuge ofFasciolasp., showing low frequency of types G and H. In the third group, most of the patterns were types E and F of group I, showing high peaks of γ-globulin fraction, and type L of group III showing the peaks in the latter half areas of γ-globulin fraction.
The cattle group having types G and H of group II showed frequently a high positive rate and high antibody titer against antigen made fromFasciolasp. in agar gel-diffusion test. A-year-long follow-up study of 19 cattle naturally infected withFasciolasp. revealed a high frequency of types G and H from November to March when there was a high positive rate and high antibody titer, suggesting Fasciolasp. infection. It was suggested that types G and H may relate to heavy infection withFasciolasp., especially the immature one.
In cases showing peaks in the first half areas of γ-globulin fraction in types G and H, a single band corresponding to γ1-globulin fraction was observed in the first half areas (anode side) of γ-globulin fraction.

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