Immunological and Electrophoretic Characteristics of Anti-SGP Reacting Protein Among Component -3, -5 and -8 Fractions of Proteose-Peptone of Bovine Milk: Evidence for the Multiple Forms
牛乳のプロテオースペプトンの成分-3,-5および-8画分に存在するAnti-SGP Reacting Proteinの免疫学的•電気泳動的特性

Choemon KANNO, Yoshiyuki OHTAKE
1981 Nihon Chikusan Gakkaiho  
The anti-SGP reacting protein, the designation for the whey protein which react with the antiserum to the soluble glycoprotein (SGP) isolated from milk fat globule membrane, was studied immunologically and electrophoretically, using the fractions obtained by gel filtration on Bio Gel A-0.5m or chromatography on DEAE-cellulose of the component-3, -5 and -8 fractions of the proteose-peptone of bovine milk. The results of analyses on quantitative simple radial immunodiffusion, double
more » ... ouble immunodiffusion, immunoelectrophoresis, and disc electrophoresis of the obtained fractions suggested that a slow migrating band and band 3 were deeply in relation with the anti-SGP reacting protein. The precipitation lines of the fractions indicated positive reaction to the anti-SGP fused completely with each other and even among the component-3, -5 and -8 on double immunodiffusion, suggesting the presence of a set of antigenic determinant group. Immunoelectrophoretic patterns of 9 fractions obtained by DEAE-cellulose chromatography of the component-3 showed that the migrating rate of the precipitation lines increased in the order of the fraction eluted through DEAE-cellulose. The results suggested that there were the multiple forms of the anti-SGP reacting protein. The anti-SGP reacting protein present in the component-5 and -8 did not correspond to all of them of the component-3 but did to some of them. It was tried to elucidate structural relationship between the anti-SGP reacting protein and SGP by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two polypeptides (band A and B), appeared to be common to both proteins. The multiple forms of the anti-SGP reacting protein seemed to be formed by intermolecular association of two major polypeptides with other minor polypeptides. There was no evidence that the anti-SGP reacting protein was derived from bovine serum. Jpn. J. Zootech. Sci., 52 (4): [282][283][284][285][286][287][288][289][290][291][292][293][294][295][296] 1981 Milk fat globule membrane (MFGM) is derived from the apical plasma membrane of the lactating mammary gland and has an important property for dispersion of fat globule in milk1,2). Of many glycoproteins constituting MFGM, the soluble glycoprotein (SGP) is a protein localized in the outer surface of fat globules3-8). It was found by KANNO and YAMAUCHI9,10) that the protein which react with the antiserum to SGP of MFGM, called as the anti-SGP reacting protein, was present in the heat-stable protein fraction of bovine milk whey: the component-3, -5 and -8 fractions of proteose-peptone. Chemical and physicochemical characteristics of the component-3 fraction, in which the anti-SGP reacting protein was mostly concentrated, were markedly different from those of SGP10). In addition, immunodiffusion tests showed that the Jpn. J. Zootech. Sci., 52 (4): 282-296
doi:10.2508/chikusan.52.282 fatcat:whkancij45fxjicn4hc7gyjgwe