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Isolation and characterization of the C3b-binding entity of C3b-receptor from human erythrocytes.

Abstract：

:Applying 2 M KBr, membranes of Ehu were solubilized. By C3-affinity chromatography an activity could be isolated that inhibited the immune adherence reaction and C3b-dependent rosette formation. Since this material did not agglutinate EAC14oxy23b we termed it monovalent C3b receptor (mC3bR). PAGE and SDS-PAGE and staining with Coomassie brilliant blue and PAS reagent revealed a single glycoprotein band with a mol. wt. of 55,000-60,000 daltons and an electrophoretic mobility comparable to ovalbumin. This mC3bR proved to be antigenetically related to gp 205 [17]. The potential of mC3bR to react with C3b-carrying particles was not destroyed by heat and trypsin treatment but by neuraminidase or periodic acid treatment suggesting that mC3bR reacted by its carbohydrate moiety with C3b. As by mC3bR, immune adherence could be inhibited by D-glucose and D-galactose but not by their optical antipodes, L-glucose and L-galactose.

journal_name

Immunol Lett

journal_title

Immunology letters

authors

Mussel HH,Ehlen T,Schmitt M,Kazatchkine MD,Neyses L,Dierich MP

doi

10.1016/0165-2478(82)90069-4

subject

Has Abstract

pub_date

1982-01-01 00:00:00

pages

1-6

issue

1

eissn

0165-2478

issn

1879-0542

pii

0165-2478(82)90069-4

journal_volume

4

pub_type

杂志文章

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