Purified method of CRP in large scale and physicochemical properties of purified CRP were studied.
Human CRP was isolated from pleural and ascitic fluids using procedure as follows; (NH
4)
2SO
4 fractionation, DEAF-cellulose (DE-52), and gel-filtration (Sephacryl S-200).
A sigle protein band was observed on disc electrophoresis and on immunoelectrophoresis suggested pure that CRP was isolated by the above procedure. It was found that the purified CRP was crystallized with ease in the process of concentration by ultra-filtration. On analytical ultracentrifugation, purified CRP was found to be 7.38 Sw
20.
From amino acid analysis, it was determined that amino acid components of this purified CRP agreeds with the result reported by Edelman et al..
Specific antibody activity of antiserum obtained from rabbits immunized by the purified CRP was confirmed by immunoelectrophoresis.
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