Multiple isoforms of the human pentraxin serum amyloid P component.
Human serum amyloid P component (SAP) isolated from 20 healthy individuals was analyzed by anion exchange chromatography and isoelectric focusing (IEF) in order to investigate the existence of multiple forms of SAP and interindividual structural differences. Anion exchange chromatography showed one major and several minor subpopulations of SAP. IEF of all SAP isolates showed a previously unreported degree of heterogeneity with six isoelectric forms (pKi range 5.5-6.1) and with minor interindividual differences in respect of isoelectric points. Total enzymatic deglycosylation of SAP reduced the number of bands in IEF to two indicating the existence of two types of polypeptide chains.
Sørensen
I J
IJ
Department of Medical Microbiology, Odense University, Denmark.
Andersen
O
O
Nielsen
E H
EH
Svehag
S E
SE
D001798:Blood Proteins / Q000737:chemistry / Q000648:ultrastructure; D002852:Chromatography, Ion Exchange; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D008297:Male; D008854:Microscopy, Electron; D015394:Molecular Structure; D000683:Serum Amyloid P-Component / Q000737:chemistry* / Q000648:ultrastructure
D001798:Blood Proteins; D000683:Serum Amyloid P-Component