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The charge-heterogeneity of human fibrinogen as investigated by 2D electrophoresis |
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| Authors: | Michelsen A E Santi C Holme R Lord S T Simpson-Haidaris P J Solum N O Pedersen T M Brosstad F |
| Affiliation: | a Research Institute for Internal Medicine, Rikshospitalet, University of Oslo, Sognsvannsveien 20, 0027 Oslo, Norway b Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA c Departments of Medicine, Microbiology and Immunology, and Pathology, University of Rochester, Rochester, NY, USA |
| Abstract: | The charge-heterogeneity of human plasma fibrinogen subunit chains was characterized by two-dimensional electrophoresis (2DE). Western blotting with antibodies specific for the γ-chain demonstrated that the γ-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, covalent γγ-dimerization by FXIIIa was not influenced by the charge-heterogeneity, and removal of the carbohydrate did not reduce the number of γ-chain pI variants. These observations suggest that the microheterogeneity of the γ-chain is a multifactorial phenomenon that is not due to physiologic modification of the glycoprotein in circulation. |
| Keywords: | Fibrinogen γ-Chain Heterogeneity Two-dimensional electrophoresis |
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