Chemical Attraction between Adults of Nippostrongylus brasiliensis: Characterization of the Substance Which Attracts Females

1977 ◽  
Vol 63 (5) ◽  
pp. 849 ◽  
Author(s):  
Thomas M. Roberts ◽  
Ralph E. Thorson
Keyword(s):  
Nippostrongylus Brasiliensis ◽  
Chemical Attraction

scholarly journals Suppression of IgE antibody production in SJL mice. III. Characterization of a suppressor substance extracted from normal SJL spleen cells.

1977 ◽  
Vol 145 (6) ◽  
pp. 1501-1510 ◽  
Author(s):  
N Watanabe ◽  
Z Ovary
Keyword(s):  
Antibody Production ◽  
High Titer ◽  
Gel Filtration ◽  
Keyhole Limpet Hemocyanin ◽  
Cell Extract ◽  
Nippostrongylus Brasiliensis ◽  
Spleen Cells ◽  
Ige Antibody ◽  
Third Stage

SJL mice were immunized with 1 microng dinitrophenylated keyhole limpet hemocyanin in 1 mg Al(OH)3. The mice were infected 21 days later with 750 third stage larvae of Nippostrongylus brasiliensis. On day 35, 14 days after infection, they were injected with 1 microng DNP-N, brasiliensis extract (Nb) in 1 mg Al(OH)3. In order to obtain high titer and persistent anti-DNP IgE antibody the mice were irradiated (540 R) 1 day after injection of DNP-Nb. Suppression of anti-DNP IgE antibody production was induced by spleen cells from normal SJL mice. Suppression of IgE antibody response is also obtained by an extract from normal SJL spleen cells. The suppressor substance from normal SJL spleen cell extract is a heat-labile protein, and is not absorbed by anti-mouse immunoglobulin. The mol wt of this substance is larger than 300,000 daltons as determined by gel filtration on Sephadex G-200, but after ultracentifugation, the supernate still has suppressive activity on IgE antibody production.

Characterization of proteolytic enzymes from larval and adult Nippostrongylus brasiliensis

Parasitology ◽  
1991 ◽  
Vol 103 (2) ◽  
pp. 305-314 ◽  
Author(s):  
J. Healer ◽  
F. Ashall ◽  
R. M. Maizels
Keyword(s):  
Proteolytic Enzymes ◽  
Nippostrongylus Brasiliensis ◽  
Fluorogenic Substrates ◽  
Intestinal Tissue ◽  
Heat Labile ◽  
Specific Uptake

Proteases from infective larval (L3) and adult stages of Nippostrongylus brasiliensis were investigated with a combination of techniques involving gelatin degradation and cleavage of fluorogenic substrates. Analysis of L3 excretory–secretory (ES) products revealed enzymes of Mr 51, 58, 79, ~ 150 and ~ 250 kDa. Inhibition profiles indicate that the major 51 kDa protease is a metallo-enzyme. Significantly, little activity was present in larval somatic extracts, suggesting the synthesis of zymogens or precursor forms prior to secretion. Adult ES contained a distinct enzyme, of 50 kDa, and a number of other proteases were detected in somatic extracts of this stage, ranging from 51 to > 300 kDa. The largest of these adult somatic enzymes is also a putative metallo-protease. While nearly all enzymes from both L3 and adult are heat labile, incubation at 100 °C generated a previously unobserved activity at 20 kDa. Furthermore, a protease of similar size may be found in uninfected rat intestinal tissue, suggesting specific uptake of a host-associated enzyme by the parasite in the form of an inactive, heat-labile complex.

Characterization of Nippostrongylus brasiliensis Infection in Different Strains of Mice

1990 ◽  
Vol 76 (3) ◽  
pp. 377 ◽  
Author(s):  
A. W. Stadnyk ◽  
P. J. McElroy ◽  
J. Gauldie ◽  
A. D. Befus
Keyword(s):  
Nippostrongylus Brasiliensis ◽  
Different Strains

scholarly journals Identification of oversulphated galactosaminoglycans in intestinal-mucosal mast cells of rats infected with the nematode worm Nippostrongylus brasiliensis

1988 ◽  
Vol 253 (3) ◽  
pp. 885-893 ◽  
Author(s):  
M Kusche ◽  
U Lindahl ◽  
L Enerbäck ◽  
L Rodén
Keyword(s):  
Mast Cells ◽  
Chondroitin Sulphate ◽  
Nippostrongylus Brasiliensis ◽  
Dermatan Sulphate ◽  
Mucosal Mast Cells ◽  
Isomeric Structures ◽  
Nematode Worm ◽  
Type Sequence ◽  
Acid Unit

The oversulphated galactosaminoglycans synthesized by rat mucosal mast cells were isolated from the small intestine of animals infected with the nematode Nippostrongylus brasiliensis, which causes proliferation of these cells. The 35S-labelled polysaccharides were degraded by digestion with chondroitinase ABC, and the structures of the disaccharide products were determined by cleavage with mercuric acetate followed by electrophoretic characterization of the resultant sulphated monosaccharides. It was concluded that about half of the disulphated disaccharide units in the polysaccharide consisted of chondroitin sulphate E-type structures [GlcA-GalNAc(4,6-di-OSO3)], in which both sulphate groups were located on the N-acetylgalactosamine unit. The remainder consisted of isomeric structures with one sulphate group on the N-acetylgalactosamine residue and one on the hexuronic acid unit and presumably represented the dermatan sulphate-type sequence [IdoA(2-OSO3)-GalNAc(4-OSO3)].

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

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