当前位置： SCI文献检索 > MOLECULAR AND BIOCHEMICAL PARASITOLOGY期刊下所有文献 > Purification, characterization, and immunochemical studies of beta-N-acetyl-D-hexosaminidase from the parasitic nematode Trichinella spiralis.

Purification, characterization, and immunochemical studies of beta-N-acetyl-D-hexosaminidase from the parasitic nematode Trichinella spiralis.

Abstract：

:The exoglycosidase, beta-N-acetyl-D-hexosaminidase was purified 600-fold from the muscle-stage larvae (L1) of Trichinella spiralis. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the purified enzyme-active fraction contained 4 polypeptides with apparent molecular weights of 100,000, 68,000, 58,000 and 54,000. The beta-N-acetyl-D-hexosaminidase corresponds to the Mr 100,000 polypeptide as demonstrated by SDS-PAGE analysis of the enzyme-stained region isolated from a non-denaturing polyacrylamide gel. In addition, rabbit antiserum to a homogeneous preparation of the Mr 100,000 polypeptide (isolated by electroelution from an SDS-PAGE gel) specifically immunoprecipitated beta-N-acetyl-D-hexosaminidase activity from an extract of L1. Isoelectrofocusing (pH 3-10) resolved 4 isoenzymes of T. spiralis beta-N-acetyl-D-hexosaminidase with isoelectric points (pI) of 5.35, 5.49, 5.63 and 5.79. The T. spiralis beta-N-acetyl-D-hexosaminidase is a glycoprotein based on its binding to lentil-lectin Sepharose affinity column and its specific binding of concanavalin A on Western blots. The IgG fraction of T. spiralis-infected mouse serum specifically immunoprecipitated T. spiralis beta-N-acetyl-D-hexosaminidase. The removal of carbohydrate from T. spiralis beta-N-acetyl-D-hexosaminidase significantly reduced its antigenicity. Immunocytochemical analysis of L1 tissue sections with polyclonal rabbit antisera to the homogeneous beta-N-acetyl-D-hexosaminidase enzyme indicated localization on cell membranes and the epicuticle.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Rhoads ML

doi

10.1016/0166-6851(88)90145-4

subject

Has Abstract

pub_date

1988-10-01 00:00:00

pages

57-69

issue

1

eissn

0166-6851

issn

1872-9428

pii

0166-6851(88)90145-4

journal_volume

31

pub_type

杂志文章

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