VARIATIONS IN THE RELATIVE PROPORTIONS OF MICROHETEROGENEOUS FORMS OF PLASMA GLYCOPROTEINS IN PREGNANCY AND DISEASE

  • 1 January 1982
    • journal article
    • research article
    • Vol. 36  (2) , 77-86
Abstract
Using lectin affinity crossed immunoelectrophoresis with concanavalin A [con A] in the first dimension and electroendosmotic elution with sugar in the second dimension, the microheterogeneity of a range of plasma proteins was examined. Of the 5 chosen proteins, .alpha.1-protease inhibitor and ceruloplasmin displayed complex patterns, with more than 4 components. .alpha.1-Antichymotrypsin was composed of 3 or 4 components while .alpha.1-acid glycoprotein and .alpha.2-HS glycoprotein displayed 2, 3 or 4 components. The number of components seen in these proteins depended on the serum sample origin. In pregnancy and in patients receiving exogenous estrogen the relative proportions of the components of all 5 proteins were altered in the direction of less con A binding; however .alpha.1-acid glycoprotein and .alpha.1-antichymotrypsin showed the greater change. In acute disorders the proportions of protein components of .alpha.1-antichymotrypsin and .alpha.1-acid glycoprotein were altered towards a higher level of con A binding components. There is no significant alteration in con A binding associated with the chronic inflammatory response to cancer and rheumatoid arthritis. There was a general reduction of con A binding in all 5 plasma proteins in conditions when there was a high blood estrogen level. This decreased affinity for con A was independent of the overall effect of the estrogen on the serum concentration of the plasma protein. The glycosylation of plasma proteins is probably under the same regulatory system.