AMINO TERMINAL SEQUENCE OF AMYLOID P-COMPONENT ISOLATED FROM SERUM
- 1 January 1978
- journal article
- research article
- Vol. 92 (1) , 78-83
Abstract
Amyloid AP (protein SAP) was isolated from human serum by affinity chromatography using specific antiserum and shown to have the same immunologic and ultrastructural characteristics as the pentagonal protein isolated from amyloid tissue (AP). Polyacrylamide gel electrophoresis in SDS [sodium dodecyl sulfate] reveals a single subunit of 25,000 daltons for both SAP and AP preparations. N-terminal amino acid sequence of this alpha globulin to 13 residues reveals complete homology with the tissue-extracted protein, suggesting that AP is incorporated into, or adsorbed onto, amyloid fibrils without biochemical alteration.This publication has 8 references indexed in Scilit:
- Evidence That C1t (Amyloid P-Component) Is Not a Subcomponent of the First Component of Complement (C1)The Journal of Immunology, 1977
- ISOLATION OF AMYLOID P COMPONENT (PROTEIN AP) FROM NORMAL SERUM AS A CALCIUM-DEPENDENT BINDING PROTEINThe Lancet, 1977
- Partial amino-acid sequences of human and rabbit C-reactive proteins: homology with immunoglobulins and histocompatibility antigens.Proceedings of the National Academy of Sciences, 1977
- Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins).Proceedings of the National Academy of Sciences, 1977
- FURTHER-STUDIES ON IDENTIFICATION OF SUBCOMPONENTS OF 1ST COMPONENT OF COMPLEMENT AFTER AFFINITY CHROMATOGRAPHY OF HUMAN-SERUM ON IGG-SEPHAROSE1977
- The Ultrastructure of C1t, a Subcomponent of the First Component of Complement: An E.M. and Ultracentrifuge StudyThe Journal of Immunology, 1976
- P-component of amyloid. Isolation from human serum by affinity chromatographyArthritis & Rheumatism, 1976
- A Protein SequenatorEuropean Journal of Biochemistry, 1967