The charge-heterogeneity of human plasma fibrinogen subunit chains was char
acterized by two-dimensional electrophoresis (2DE). Western blotting with a
ntibodies specific for the gamma -chain demonstrated that the gamma -chains
focus at varying isoelectric points (pI). This microheterogeneity was also
observed in fibrinogen secreted from hepatocytic cells and in recombinant
fibrinogen expressed in Chinese hamster ovary (CHO) cells. Further, covalen
t yy-dimerization by FXIIIa was not influenced by the charge-heterogeneity,
and removal of the carbohydrate did not reduce the number of gamma -chain
pi variants. These observations suggest that the microheterogeneity of the
gamma -chain is a multifactorial phenomenon that is not due to physiologic
modification of the glycoprotein in circulation. (C) 2000 Elsevier Science
Ltd. All rights reserved.