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Isolation of a pentraxin-like protein from rainbow trout serum

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  • Department of Medical Microbiology and Immunology
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).
Original languageEnglish
JournalDevelopmental & Comparative Immunology
Volume19
Issue4
Pages (from-to)305-14
Number of pages10
ISSN0145-305X
Publication statusPublished - 1995

    Research areas

  • Alpha-Globulins, Amino Acid Sequence, Animals, C-Reactive Protein, Glycosylation, Humans, Molecular Sequence Data, Molecular Weight, Oncorhynchus mykiss, Protein Binding, Rabbits, Sepharose, Sequence Homology, Amino Acid, Serum Amyloid P-Component

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