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Glycoprotein characterization of the gelatinous matrix in the root-knot nematode Meloidogyne javanica
Year:
1993
Source of publication :
Journal of Nematology
Authors :
Sharon, Edna
;
.
Spiegel, Yitzhak
;
.
Volume :
25
Co-Authors:
Facilitators :
From page:
585
To page:
589
(
Total pages:
5
)
Abstract:

Proteinaceous components of freshly formed gelatinous matrix (GM) of the root-knot nematode Metoidogyne javanica were analyzed. Under reducing conditions, the prominent protein fragments had molecular weights of 26 to 66 kDa and 150 to >200 kDa, and most were glycosylated. Most of the fragments were digested by proteinase K, and fewer by trypsin. The lectins soybean agglutinin (SBA), Ulex europaeus agglutinin, and wheat germ agglutinin labeled the higher molecular weight bands (i.e., >200 kDa). SBA labeled additional protein fractions between 26 and 66 kDa. Although Bandeiraea simplicifolia lectin and Concanavalin A did not label bands on the Western blot, they did label the GM in the dot blot technique. Analysis of amino acids and amino sugars in the GM revealed an unusually high amount of ammonia and galactosamine moieties.

Note:
Related Files :
Gelatinous matrix
glycoprotein
lectin
Meloidogyne javanica
Nematoda
nematode
Protein
proteins
Root-knot nematode
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More details
DOI :
Article number:
0
Affiliations:
Database:
PubMed
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
38950
Last updated date:
02/03/2022 17:27
Creation date:
10/01/2019 11:52
Scientific Publication
Glycoprotein characterization of the gelatinous matrix in the root-knot nematode Meloidogyne javanica
25
Glycoprotein characterization of the gelatinous matrix in the root-knot nematode Meloidogyne javanica

Proteinaceous components of freshly formed gelatinous matrix (GM) of the root-knot nematode Metoidogyne javanica were analyzed. Under reducing conditions, the prominent protein fragments had molecular weights of 26 to 66 kDa and 150 to >200 kDa, and most were glycosylated. Most of the fragments were digested by proteinase K, and fewer by trypsin. The lectins soybean agglutinin (SBA), Ulex europaeus agglutinin, and wheat germ agglutinin labeled the higher molecular weight bands (i.e., >200 kDa). SBA labeled additional protein fractions between 26 and 66 kDa. Although Bandeiraea simplicifolia lectin and Concanavalin A did not label bands on the Western blot, they did label the GM in the dot blot technique. Analysis of amino acids and amino sugars in the GM revealed an unusually high amount of ammonia and galactosamine moieties.

Scientific Publication
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