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The association of the subunits of component C3 of hagfish complement is unstable and leads to novel degradation during electrophoresis
Author(s) -
Fujii Tamotsu,
Kunisada Satomi
Publication year - 1997
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/icb.1997.88
Subject(s) - hagfish , covalent bond , chemistry , biochemistry , molecule , thioester , protein subunit , biophysics , biology , enzyme , organic chemistry , vertebrate , gene
An opsonic molecule that is designated the third component of hagfish complement (HC3), and a fragment of HC3 known as HC3b have recently been identified in the hagfish, Eptatretus burgeri. These proteins were purified from plasma and generated a set of several bands and/or smears during SDS‐PAGE under standard, non‐reducing conditions. Two‐dimensional electrophoretic analysis of the proteins under non‐reducing and reducing conditions revealed the breakdown of polypeptides at the site of a thioester bond and the concomitant partial release of a split product, depending on the weak covalent or non‐covalent association of polypeptide chains, in a large fraction of molecules of HC3 during SDS‐PAGE. Moreover, the heterogeneity of HC3b can be ascribed to the different configurations of subunits. A similar phenomenon was not observed in the case of lamprey C3, even though breakdown of polypeptides at a thioester bond did occur in some molecules.