Solubilization of active complement receptor type 1 (CR1) from human erythrocyte stroma with trypsin and its purification.

Abstract:

:Mild trypsinization of human erythrocyte stroma solubilized CR1 (complement receptor type 1, C3b/C4b receptor) without significant loss of decay-accelerating activity to C5 convertases on hemolytic intermediate cells (EAC 1-3b, P). The solubilized CR1 was purified using DEAE-Sephacel, C3-Sepharose, and anti-CR1-Sepharose column chromatographies. The purified material showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing conditions, and its molecular weight was determined to be 175K, about 20K smaller than native CR1. Because the purified sample was separated into the several segments by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions, the molecule is considered to be nicked and those segments are associated by disulfide bonds. These results mean that a large portion of the CR1 molecule is present outside of the plasma membrane of erythrocytes, and the intramembranous and cytoplasmic domains are not necessary for decay-accelerating activity.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Sugita Y,Nakano Y,Tomita M

doi

10.1093/oxfordjournals.jbchem.a121823

subject

Has Abstract

pub_date

1986-11-01 00:00:00

pages

1193-200

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

100

pub_type

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