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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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Volume 383, Issue 12


Identification and Characterization of an IgG Binding Protein in the Secretion of the Rat Coagulating Gland

B. Wilhelm / C. Keppler / A. Henkeler / M. Schilli-Westermann / D. Linder / G. Aumüller / J. Seitz
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.221


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 SDSPAGE under reducing conditions. Furthermore, the 115 kDa protein is glycosylated, and carries Man, GlcNAc, Gal, Fuc and sialic acid residues. For identification, Nterminal 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.

About the article

Published Online: 2005-06-01

Published in Print: 2002-12-09

Citation Information: Biological Chemistry, Volume 383, Issue 12, Pages 1959–1965, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.221.

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