Isolation and characterization of rainbow trout (Oncorhynchus mykiss) serum amyloid P component (SAP)
We purified a Ca(2+)-dependent agarose-binding protein from rainbow trout (Oncorhynchus mykiss) sera. SDS-PAGE analysis showed the possibility that the purified protein was a polymer with a molecular weight of over 100,000 composed of covalently-bounded 32-kDa subunits. N-terminal twenty amino acid sequence of the 32-kDa protein showed partial homology with other known serum amyloid P components (SAPs) including plaice (Pleuronectes platessa) (indicated 40% homology), human (55%), hamster (45%), rat and mouse (40%) SAPs. In electron micrographs the 32-kDa protein was observed as pentameric disc-like structure. On the basis of the results, the 32-kDa agarose-binding protein of rainbow trout was concluded to belong to pentraxin family and to be a SAP homologue.
Murata
M
M
Department of Epizootiology, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Onuma
M
M
Kodama
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D005432:Flounder; D006801:Humans; D051379:Mice; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017686:Oncorhynchus mykiss / Q000097:blood* / Q000235:genetics; D011487:Protein Conformation; D051381:Rats; D017386:Sequence Homology, Amino Acid; D000683:Serum Amyloid P-Component / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D013045:Species Specificity
D000683:Serum Amyloid P-Component