scholarly journals Biochemical changes in developing embryos of Schistocerca gregaria (Orthoptera: Acrididae) induced by pheromone produced by ovipositing gregarious females

2015 ◽  
Vol 35 (03) ◽  
pp. 125-131
Author(s):  
Fathiya M. Khamis ◽  
Paul O. Mireji ◽  
Ellie O. Osir ◽  
Mabel O. Imbuga ◽  
Ahmed Hassanali
Keyword(s):  
Gel Electrophoresis ◽  
Time Course ◽  
Schistocerca Gregaria ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Gene Expressions ◽  
Protein Gel ◽  
Profile Matching ◽  
Signalling Cascades ◽  
Different Levels

Trans-generational transfer of gregarious-phase traits in the desert locustSchistocerca gregaria(Forskål, 1775) is mediated by primer gregarizing pheromonal signals produced by ovipositing females that experience crowding. We monitored time-course proteomic events in eggs from solitary-reared locusts that had been exposed for 1, 3, 5, 7, 10 and 12 days to different levels of the sand-associated gregarizing signal originating from 0, 3, 5 or 10 ovipositions by crowd-reared females. Evidence for the phase transition was sought by comparing the protein patterns of embryos thus exposed with those from crowd-reared (gregarious) controls; this comparison was continued until the stage of the first instars. Expressed proteins were analysed by two-dimensional protein gel electrophoresis, and patterns from the different treatments within stages were compared by profile matching andχ2analyses. Eggs derived from crowd- and solitary-reared females showed essentially similar protein patterns at early stages of embryogenesis; however, mature stages (particularly, days 10 and 12) and hatchlings demonstrated significantly different patterns. Protein patterns of eggs from solitary-reared females that were incubated in sand contaminated with the pheromonal signal and of the hatchlings that emerged were similar to those derived from gregarious females and dependent on the level of the pheromone to which the embryos had been exposed. The results confirm the gregarizing effect of the signal and constitute a useful basis for unravelling the mechanism of the signalling cascades associated with gene expressions triggered by the pheromone.

Variation in goat fibre protein

1989 ◽  
Vol 40 (3) ◽  
pp. 675 ◽  
Author(s):  
DJ Tucker ◽  
AHF Hudson ◽  
A Laudani ◽  
RC Marshall ◽  
DE Rivett
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Wool Fibre ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Cashmere Goats

The proteins from a range of cashmere, mohair, angoratcashmere crossbred and wool fibre samples were extracted at pH 8 with 8 M urea containing dithiothreitol, and were then radiolabelled by S-carboxymethylation using iodo(2-14C) acetate. The proteins from each sample were examined by two dimensional polyacrylamide gel electrophoresis in which the separation in the first dimension was according to charge at pH 8.9 and in the second dimension according to apparent molecular weight in the presence of sodium dodecyl sulfate. After electrophoresis the proteins were detected by fluorography. Protein differences in keratin samples from some individual goats existed, although the overall protein patterns were similar. None of the differences were consistent with any one goat fibre type. The protein patterns obtained for fibre samples from individual cashmere goats showed some differences when compared to those found for commercial blends from the same country of origin, indicating that blending can mask any animal-to-animal variation. While the electrophoretic technique does not unequivocally distinguish between cashmere, mohair and angora/cashmere crossbred fibres it does differentiate between wool and goat fibres.

Two-dimensional protein gel electrophoresis: A powerful tool in experimental pharmacology and toxicology

1995 ◽  
Vol 31 ◽  
pp. 376
Author(s):  
L. Aicher ◽  
M. Varela ◽  
D. Wahl ◽  
N.L. Anderson ◽  
J.P. Hofmann ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Protein Gel ◽  
Experimental Pharmacology ◽  
Pharmacology And Toxicology

Proteins in normal, irradiated, and postmortem human brain quantitatively compared by using two-dimensional gel electrophoresis.

1984 ◽  
Vol 30 (12) ◽  
pp. 1989-1995 ◽  
Author(s):  
R K Narayan ◽  
W E Heydorn ◽  
G J Creed ◽  
P L Kornblith ◽  
D M Jacobowitz
Keyword(s):  
Cerebral Cortex ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Relative Molecular Mass ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Human Cerebral Cortex ◽  
Postmortem Human Brain ◽  
Two Dimensional Gel Electrophoresis ◽  
Fresh Frozen

Abstract Using a combination of two-dimensional gel electrophoresis (2DE), silver staining, and computerized densitometry, we studied protein patterns in human cerebral cortex: normal fresh-frozen, fresh-frozen but previously irradiated, and post-mortem. The relative molecular mass of the resolved proteins ranged from 14 400 to 100 000, the isoelectric points from 4.75 to 7.0. The pattern of proteins (six of them identified) was essentially the same for all three groups. However, computerized densitometry demonstrated significant alterations in the density of several spots in the irradiated and postmortem groups as compared with the normal controls. Irradiated cortex showed statistically significant changes in only six spots (three increased and three decreased in density); postmortem material showed 20 altered spots (16 diminished and four increased). Evidently normal human cerebral cortex has a consistent protein pattern on 2DE, which is quantitatively (but not qualitatively) altered in irradiated and postmortem material. These findings provide a point of reference against which proteins from abnormal brain material can be compared, both qualitatively and quantitatively.

Induction of Heat-Shock Protein (hsp) by Moxibustion

1995 ◽  
Vol 23 (03n04) ◽  
pp. 327-330 ◽  
Author(s):  
Kazuko Kobayashi
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Hsp 70 ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
Hip Muscle ◽  
And Control ◽  
Muscular Tissues

Rats were treated by moxibustion at the point of hip muscle, and intramuscular temperature was kept at 40°C for 15 minutes. The rats were sacrificed under deep anesthesia and the muscular tissues were excised immediately, three hours and 24 hours after stimulation. Proteins were extracted from the homogenized and centrifuged tissues of the stimulated rats and control rats. Two-dimensional gel electrophoresis of the proteins was carried out. Heat-shock protein (hsp) with molecular weight of 70,000 (hsp 70), 85,000 (hsp 85) and 100,000 (hsp 100) was detected in rats sacrificed three hours after the stimulation by moxibustion. Protein patterns were analyzed and the ratios of the hsps were obtained.

Two-dimensional protein patterns of tomato (Lycopersicon esculentum Mill.) seeds; effects of isolation procedure and imbibition

1994 ◽  
Vol 4 (3) ◽  
pp. 275-283 ◽  
Author(s):  
J. H. W. Bergervoet ◽  
H. L. Kraak ◽  
C. H. R. De Vos ◽  
R. J. Bino
Keyword(s):  
Lycopersicon Esculentum ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
General Picture ◽  
Isolation Methods ◽  
Lysis Buffer

AbstractA computer-aided comparison of tomato (Lycopersicon esculentum Mill.) seed protein patterns, obtained after two-dimensional gel electrophoresis, was made for three different extraction procedures: TCA acetone/lysis buffer, lysis buffer only and modified Laemmli/lysis buffer. Comparison of the isolation methods showed that about half of the amount of proteins detected was common in each method. Also, proteins specific to some isolation methods were detected. Protein synthesis during imbibition was monitored using 35S-methionine. After labelling the proteins were extracted using TCA acetone/lysis buffer. Following two-dimensional gel electrophoresis the gels were first silver stained, to give a general picture of all proteins present in the seed, then the gels were exposed to a film for autoradiography. Comparison of the in vivo-synthesized protein patterns and the silver-stained proteins revealed that from day 0 to day 1 the protein pattern was changed but the total number of different spots was similar. After 1 day of imbibition, the number of protein spots increased greatly and the protein pattern changed again.

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