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  Occupational safety and health series

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  v. 5-13, 15-16, 18, 20-25, 1964-68, [1969-70].

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  P-component of amyloid. Isolation from human serum by affinity chromatography.

  Benson MD, Skinner M, Shirahama T, Cohen AS.

  Arthritis Rheum. 1976 Jul-Aug;19(4):749-54.

  Human amyloid P-component was isolated from plasma by affinity chromatography utilizing antiserum to tissue P-component coupled to Sepharose 4B. Characterization and comparison of the isolated P-component proteins from tissue and plasma demonstrated immunologic identity and identical RF values of polyacrylamide disk gel electrophoresis. Amino acid analyses of P-components from two individual plasmas were comparable, but some variations from tissue P-component were noted. Attempts to perform amino acid sequencing on the plasma protein were unsuccessful. Electron microscopic studies revealed that the plasma P-component had a pentagonal ultrastructure identical to the tissue P-component. These studies compared similarities of tissue and plasma P-components and revealed the unique pentagonal ultrastructure of the plasma protein.

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