Lectin binding analysis of Argas polonicus tissue glycoproteins
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články
PubMed
1858292
DOI
10.1016/0304-4017(91)90133-g
PII: 0304-4017(91)90133-G
Knihovny.cz E-zdroje
- MeSH
- antigeny analýza MeSH
- epidermis chemie MeSH
- glykoproteiny analýza MeSH
- klíšťata analýza MeSH
- larva analýza MeSH
- lektiny analýza MeSH
- malpighické trubice chemie MeSH
- oligosacharidy analýza MeSH
- pohlavní orgány chemie MeSH
- slinné žlázy chemie MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- antigeny MeSH
- glykoproteiny MeSH
- lektiny MeSH
- oligosacharidy MeSH
Proteins of the Malpighian tubules (MT), midgut tissue (MG), salivary glands (SG), internal reproductive organs (RO), epidermis (EP), cerebral ganglion (CG), rectal ampulla (RA) and larval homogenate (LA) of Argas (Argas) polonicus were studied for their antigenicity and lecin affinity using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), immunoblotting, lectin affinoblotting and enzyme-linked lectin sorbentassay (ELLSA) techniques. A glycoprotein of 305 kDA was found in all tissues studied. All low molecular weight antigenic proteins recognized by anti-larval immune pigeon serum, except for one of 35 kDA, i.e. the 19-, 21-, 23-, 27-, 34-, and 46- kDa proteins, were shown to be glycoproteins. The glycosylation was shown to be N-linked in all of these antigens, but O-type glycosylation was also demonstrated in the 34-kDa glycoprotein. The correlation between the glycosylation and antigenicity of these proteins is also discussed.
Citace poskytuje Crossref.org
A bite so sweet: the glycobiology interface of tick-host-pathogen interactions
