Identification and characterization of an IgG binding protein in the secretion of the rat coagulating gland.
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.
Wilhelm
Beate
B
Institut für Anatomie und Zellbiologie, Philipps-Universität, D-35037 Marburg, Germany.
Keppler
Claudia
C
Henkeler
Anne
A
Schilli-Westermann
Margret
M
Linder
Dietmar
D
Aumüller
Gerhard
G
Seitz
Jürgen
J
D000595:Amino Acid Sequence; D000606:Amino Sugars / Q000032:analysis; D000818:Animals; D015153:Blotting, Western; D002460:Cell Line; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D007074:Immunoglobulin G / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D011467:Prostate / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D020133:Reverse Transcriptase Polymerase Chain Reaction
D000606:Amino Sugars; D007074:Immunoglobulin G