Jensen L E, Petersen T E, Thiel S, Jensenius J C
Department of Medical Microbiology and Immunology, University of Aarhus, Denmark.
Dev Comp Immunol. 1995 Jul-Aug;19(4):305-14. doi: 10.1016/0145-305x(95)00010-q.
Serum amyloid P-component (SAP) is a glycoprotein consisting of five or ten noncovalently associated identical subunits of molecular weight 19,000-30,000. Herein we report the isolation and partial characterization of a SAP-like protein from rainbow trout serum. The protein was isolated by calcium-dependent binding to Sepharose followed by ion-exchange and size-exclusion chromatography. Rabbit antibody against human SAP reacted with the trout protein and the NH2-terminal sequence of 16 amino acids showed 60% identity with the first 15 residues of human SAP. SDS-PAGE and endoglycosidase treatment indicated that the trout protein is a glycoprotein in which five or six subunits are linked by disulphide bonds. The subunits have a molecular weight of 37,000 of which approximately 13% is due to carbohydrate. We propose to name the trout protein sulphide linked SAP (SL-SAP).