Identification and characterization of an IgG binding protein in the secretion of the rat coagulating gland

Biological Chemistry
B WilhelmJürgen Seitz


A merocrine released protein (named 115k protein) was highly enriched from the secretion of the rat coagulating gland. The protein has a molecular mass of 115 kDa as calculated by SDS-PAGE under reducing conditions. Furthermore, the 115 kDa protein is glycosylated, and carries Man, GlcNAc, Gal, Fuc and sialic acid residues. For identification, N-terminal amino acid and nucleotide sequence analyses were performed. The sequences obtained showed 86 to 100% identity with human and mouse IgGFc binding proteins. The functional capacity of IgG binding of the 115 kDa protein was shown by overlay experiments, indicating its membership in the IgG binding protein family.


Jan 1, 1985·Annual Review of Biochemistry·R Kornfeld, S Kornfeld
Jan 1, 1980·Annual Review of Biochemistry·J E Folk
Jan 1, 1984·Molecular and Cellular Biochemistry·H G Williams-Ashman
Jun 13, 1997·The Journal of Biological Chemistry·N HaradaM Morikawa
May 9, 1998·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·B WilhelmJ Seitz
Feb 18, 1999·Cell and Tissue Research·S GroosG Aumüller
Nov 5, 1999·The Journal of Biological Chemistry·J Perez-Vilar, R L Hill
Nov 24, 1999·Annals of Anatomy = Anatomischer Anzeiger : Official Organ of the Anatomische Gesellschaft·G AumüllerJ Seitz

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