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Characterization of body louse midgut proteins recognized by resistant hosts
Year:
1996
Source of publication :
Medical and Veterinary Entomology
Authors :
Ben-Yakir, David
;
.
Volume :
10
Co-Authors:
Ochanda, J.O., Department of Biochemistry, University of Nairobi, Kenya
Mumcuoglu, K.Y., Department of Parasitology, Hebrew University, Hadassah Medical School, Jerusalem, Israel, Department of Parasitology, Hebrew University, Hadassah Medical School, P.O. Box 12272, 91120 Jerusalem, Israel
Ben-Yakir, D., Department of Parasitology, Hebrew University, Hadassah Medical School, Jerusalem, Israel
Okuru, J.K., Department of Biochemistry, University of Nairobi, Kenya
Oduol, V.O., Department of Biochemistry, University of Nairobi, Kenya
Galun, R., Department of Parasitology, Hebrew University, Hadassah Medical School, Jerusalem, Israel
Facilitators :
From page:
35
To page:
38
(
Total pages:
4
)
Abstract:
The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 1·17 kDa, when analysed by SDS-PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F1, F2, F3, and F4) when resolved on a 18% SDS-PAGE. The F1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.
Note:
Related Files :
Animal
Animals
Female
Immunogens
Male
proteins
Rabbits
Vaccine
Show More
Related Content
More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27773
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:33
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Scientific Publication
Characterization of body louse midgut proteins recognized by resistant hosts
10
Ochanda, J.O., Department of Biochemistry, University of Nairobi, Kenya
Mumcuoglu, K.Y., Department of Parasitology, Hebrew University, Hadassah Medical School, Jerusalem, Israel, Department of Parasitology, Hebrew University, Hadassah Medical School, P.O. Box 12272, 91120 Jerusalem, Israel
Ben-Yakir, D., Department of Parasitology, Hebrew University, Hadassah Medical School, Jerusalem, Israel
Okuru, J.K., Department of Biochemistry, University of Nairobi, Kenya
Oduol, V.O., Department of Biochemistry, University of Nairobi, Kenya
Galun, R., Department of Parasitology, Hebrew University, Hadassah Medical School, Jerusalem, Israel
Characterization of body louse midgut proteins recognized by resistant hosts
The human body louse, Pediculus humanus, showed eighteen midgut proteins ranging between 12 and 1·17 kDa, when analysed by SDS-PAGE electrophoresis. Seven of them (12 kDa, 17 kDa, 29 kDa, 35 kDa, 40 kDa, 55 kDa and 97 kDa) were major bands based on their intensity of staining. The immunization of rabbits with a midgut extract elicited the production of protective polyclonal antibodies. These antibodies reacted strongly with all major midgut proteins as well as with 63 kDa and 117 kDa proteins when tested by the Western blot technique. The analysis of the proteins revealed that the 12 kDa, 25 kDa, 29 kDa, 35 kDa, 45 kDa, 87 kDa and 97 kDa proteins are glycosylated and none of them contained a lipid moiety. By electroelution, the proteins of 35 kDa and 63 kDa were purified. On trypsinization, the proteins of 35 kDa and 63 kDa produced four major fragments (F1, F2, F3, and F4) when resolved on a 18% SDS-PAGE. The F1 fragment of the 35 kDa protein reacted with the polyclonal antibodies by the immunoblot technique.
Scientific Publication
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