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Structural, immunological and functional comparisons of factor H, rheumatoid arthritis protein (RHP), and its apparent normal counterpart (N-RHP).

Abstract：

:The isolation and characterization of two human serum proteins, RHP and N-RHP, are described. N-RHP appears to be the normal counterpart of RHP which is found at elevated levels in sera of patients with rheumatoid arthritis [Rosano et al. (1988b) Inflammation 12, 351 - 360]. Although both proteins crossreact with anti-Factor H and have identical N-terminal amino acid sequences, they differ from Factor H in pI, solubility at low ionic strength, and in glycosylation. RHP differs from Factor H and N-RHP in antigenicity in the rabbit, in effect on the C1q-anti-C1q precipitin reaction, and in ability to disaggregate C1, the first component of the complement system. Removal of RHP, N-RHP and Factor H from binding to C1q is a prerequesite for separation of RHP and N-RHP from Factor H by anion exchange chromatography and isoelectric focusing. The finding of uniquely demonstrable RHP activity (enhancement of C1q-anti-C1q precipitin activity) in unfractionated sera from patients with rheumatoid arthritis, but not in normal sera, suggests that RHP is not an artefact of Factor H produced during isolation.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Hurwitz C,Rosano CL,Hechemy KE,Weber P,Parhami N

doi

10.1016/0161-5890(95)00068-2

subject

Has Abstract

pub_date

1995-11-01 00:00:00

pages

1259-69

issue

16

eissn

0161-5890

issn

1872-9142

pii

0161589095000682

journal_volume

32

pub_type

杂志文章

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