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Isolation and characterization of a human alternative complement pathway-inhibiting protein from larval hemolymph of the silkworm, Bombyx mori.

Abstract：

:An alternative complement pathway-inhibiting protein (ACPIP), which inhibits the activation of the alternative complement pathway (ACP) of the human serum, was isolated from larval hemolymph of the silkworm, Bombyx mori, by using ammonium sulfate fractionation and column chromatographies to homogeneity. About 400microg of ACPIP was routinely obtained from 20ml hemolymph. The purified ACPIP preparation consisted of two distinct polypeptides (34 and 32kDa) on SDS-PAGE. The amino acid compositions of the two polypeptides were nearly identical; 21% of the amino acid residues were acidic. The amino terminal amino acid sequences up to 20 residues in these two polypeptides were also identical. Addition of the ACPIP to human serum resulted in a dose-dependent inhibition of the hemolysis of intact rabbit erythrocytes via the ACP, whereas in no inhibition of hemolysis of sensitized-sheep erythrocytes (EA) via the classical pathway.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Sekijima Y,Fujikura Y,Hiyama T,Maenaka T,Uda A

doi

10.1016/s0145-305x(00)00046-x

keywords:

subject

Has Abstract

pub_date

2001-03-01 00:00:00

pages

89-100

issue

2

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(00)00046-X

journal_volume

25

pub_type

杂志文章

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