Biochemical properties of a 24 kilodalton membrane glycoprotein antigen complex from Schistosoma mansoni.

Abstract:

:Antibodies were affinity purified from crude antiserum by elution from the 24 kDa region of preparative one-dimensional Western blots containing immobilized adult Schistosoma mansoni inner bilayer membrane proteins. They were shown to be specific for a single acidic polypeptide complex, Smgp24, following immunoblotting from two-dimensional polyacrylamide gels. These antibodies were then used to detect the presence of the Smgp24 complex in fractions prepared from lectin affinity chromatography, phase separation in Triton X-114 and chemical and enzymatic carbohydrate modification treatments. The 24 kDa antigen was bound and specifically eluted from both concanavalin A and lentil lectin affinity matrices. In addition, the electrophoretic mobility of the antigen was shifted to approximately 20 kDa after treatment with endoglycosidase F and N-glycanase, but was not appreciably altered following treatment with endoglycosidase H, neuraminidase, or sodium meta-periodate. The 20 kDa species produced by endoglycosidase F or N-glycanase treatment no longer bound to the lectin affinity resins. The Smgp24 complex also partitioned almost quantitatively into the detergent-enriched phase after phase separation in Triton X-114 solutions. These results indicate that the Smgp24 complex is an antigenic integral membrane glycoprotein and may consist of a single polypeptide backbone which is extensively post- or co-translationally modified.

journal_name

Mol Biochem Parasitol

authors

Karcz SR,Barnard BJ,Podesta RB

doi

10.1016/0166-6851(88)90167-3

subject

Has Abstract

pub_date

1988-11-01 00:00:00

pages

163-71

issue

2

eissn

0166-6851

issn

1872-9428

pii

0166-6851(88)90167-3

journal_volume

31

pub_type

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