Protein content and electrophoretic profile of insect galls on susceptible and resistant host plants of Bauhinia brevipes Vogel (Fabaceae)

2011 ◽  
Vol 59 (6) ◽  
pp. 509 ◽  
Author(s):  
Michelle de Lima Detoni ◽  
Eveline Gomes Vasconcelos ◽  
Ana Carolina Ribeiro Gomes Maia ◽  
Michélia Antônia do Nascimento Gusmão ◽  
Rosy Mary dos Santos Isaias ◽  
...  
Keyword(s):  
Hypersensitive Reaction ◽  
Biochemical Alterations ◽  
Physiological Processes ◽  
Abaxial Leaf Surface ◽  
Sds Page ◽  
Specific Proteins ◽  
Work Samples ◽  
Bauhinia Brevipes ◽  
Gall Induction ◽  
Gall Inducer

Gall induction, mediated by insect-herbivore chemical stimuli, is the result from anatomical and biochemical alterations in the host-plant tissues that provides shelter, food and defence against natural enemies and the harsh environment to the gall inducer. Schizomya macrocapillata Maia (Diptera, Cecidomyiidae) induces galls on Bauhinia brevipes Vogel (Fabaceae); the galls are spherical, with long reddish hairs that cover the adaxial wall surface of the gall, and a protuberance is observed on the abaxial leaf surface. Some plants are resistant to gall formation and, in many cases, this formation is inhibited by hypersensitive reaction. In the present work, samples from different parts of the non-galled and galled tissues from resistant and susceptible plants were carefully dissected. Indicating elevated metabolic activity, the protein concentration was 1.5–4.5-fold higher in the abaxial portion of the galls than in any other tissues, regardless of whether the galls were from resistant or susceptible plants. Different tissues from susceptible and resistant plants had distinct protein concentrations, and the fractionation of the proteins by SDS–PAGE and silver-staining showed shared and/or specific polypeptides. We hypothesise that specific proteins, possibly from distinct metabolic pathways, are involved in the physiological processes that determine whether the plant shows total and/or partial host resistance to the galling-insect attack.

scholarly journals The Reactivity and Allergenic Potential of Hazelnut Peptides

2013 ◽  
Vol 70 (1) ◽  
pp. 25
Author(s):  
Lavinia Florina Calinoiu ◽  
Dan Cristian Vodnar ◽  
Carmen Socaciu
Keyword(s):  
Proteolytic Enzymes ◽  
Peptide Fragments ◽  
Dot Blot ◽  
Specific Antibodies ◽  
Allergenic Potential ◽  
Sds Page ◽  
Allergenic Proteins ◽  
Life Threatening ◽  
Specific Proteins ◽  
Sensitive Method

The aim of this paper was to focus on proteins present in some food products, like hazelnuts and to investigate their allergenic potential. Several techniques were used to characterize these extracted proteins, with respect to their composition, degradability by digestive proteolytic enzymes and their reactivity with specific antibodies. It was important to analyse which proteins were present in the hazelnuts, to see if there were proteins present to trigger an allergic reaction and if the digestion enzymes trypsin and pepsin influence the presence of the (allergic) protein compounds. Allergies to tree nuts and seeds can cause life-threatening and sometimes fatal reactions. To examine the properties of Hazelnut protein it was important to solubilize it by extraction. After extraction, it was investigated how hazelnut protein can be modified by proteases and what the effect was on the immune reaction. The Bradford method is a fast and sensitive method to determine the concentration of soluble protein. When the Bradford reagent (Coomassie Brilliant Blue) binds to the protein, the colour changes from red to purple and the absorption maximum changes from 495 to 595 nm. The value obtained as the final concentration of proteins was 7.3495. SDS-PAGE is a method to separate mixtures of proteins by electrophoresis. Protein molecules are negatively charged by binding of SDS molecules; subsequently they are separated in an electric field. Their differences in size (molecular weight) leads to separation. In this case the method is used to follow proteolytic degradation of hazelnut proteins (allergens) by intestinal proteases (trypsin, pepsin). A different, more specific and sensitive method is immunoblotting (Western Blot) in which the SDS-PAGE separated proteins are transferred from the gel to a membrane and specific antibodies are used in a series of reactions to visualize specific allergens on this membrane. The remarked spots represented a positive identification of allergenic proteins. This means that peptide fragments of various size, produced during the digestion of a protein can still be immunological active. As it was shown there was still reactivity between proteins and specific antibodies. The Dot Blot is a simple immunoblotting technique used to detected specific proteins in a mixture of different proteins and/or other molecules. No separation technique prior to the actual immuno-detection is necessary. Also, Dot Blot confirmed the presence of allergenic proteins made visible through the light spots on the membrane.

Immunological Identification of Organ Specific Proteins and Transcripts in Developing Barley Grains

1993 ◽  
Vol 48 (7-8) ◽  
pp. 609-615
Author(s):  
Helge Klungland ◽  
Marie Bosnes
Keyword(s):  
Specific Protein ◽  
Barley Grain ◽  
Starchy Endosperm ◽  
Sds Page ◽  
Organ Specific ◽  
Specific Proteins ◽  
Barley Grains ◽  
Immunological Identification

In vitro translated proteins from poly(A+)RNA of immature barley starchy endosperm and embryos were immunoadsorbed with antibodies raised against proteins of aleurone layers, starchy endosperm and embryos. Four starchy endosperm and eight embryo specific transcripts were detected. In addition, several mRNA s were restricted to only two of the three tis­sues.Comparing SDS-PAGE patterns of the in vivo protein extracts against which the antibodies were raised, four aleurone, six starchy endosperm and four embryo-specific protein bands were detectable. As for the in vitro translated proteins, several in vivo protein bands were here present in only two of the three tissues. Of eight known barley grain proteins for which antibodies were available, only three were present in developing embryos.

Developmental changes in proteins and glycoproteins revealed by direct radio-iodination of viable Taenia saginata larvae

Parasitology ◽  
1989 ◽  
Vol 99 (2) ◽  
pp. 265-274 ◽  
Author(s):  
G. W. P. Joshua ◽  
L. J. S. Harrison ◽  
M. M. H. Sewell
Keyword(s):  
Developmental Changes ◽  
Infected Cattle ◽  
Taenia Saginata ◽  
Diagnostic Significance ◽  
Isotope Labelling ◽  
Antigenic Characterization ◽  
Lentil Lectin ◽  
Sds Page ◽  
Specific Proteins

SummaryDirect surface I radio-isotope labelling techniques and SDS—PAGE analysis were used to compare the proteins and lentil—lectin adherent glycoproteins of the bovine stage of viable Taenia saginata larvae at three points in their development, the invasive oncospheres, immature (4-week-old) and mature (12 to 16-week-old) cysticerci. Some proteins and glycoproteins were present on all three of the ages of the parasite examined but there were also distinct age-specific proteins and glycoproteins detected on oncospheres and 4-week-old cysticerci and a marked difference between the protein/glycoprotein profiles of the parasite was apparent at these earlier stages of development and the mature cysticerci. The latter were characterized by the presence of high, 160–200 kDa molecular weight, lysine rich, glycoproteins, whereas small 16 and 18 kDa glycoproteins and a reduction-sensitive 23 kDa glycoprotein were first detected on 4-week-old immature cysticerci. Antigenic characterization of the isotope-labelled proteins and glycoproteins by immunoprecipitation against a panel of clinically defined bovine sera combined with SDS–PAGE analysis indicated that relatively few proteins were precipitated by sera from T. saginata-infected cattle as compared to the glycoproteins. However, both protein and glycoprotein antigens of possible protective and/or diagnostic significance were identified from oncospheres and cysticerci.

Milk Composition in a Field Population of Red Kangaroos, Macropus Rufus (Desmarest) (Macropodidae: Marsupialia)

1996 ◽  
Vol 44 (2) ◽  
pp. 165 ◽  
Author(s):  
E Muths
Keyword(s):  
Whey Proteins ◽  
Milk Composition ◽  
Field Population ◽  
Sds Page ◽  
Macropus Rufus ◽  
Total Milk ◽  
Specific Proteins ◽  
Milk Solids

The composition of milk from early pouch life (0-40 days) to weaning (360 days) was determined in samples collected from a field population of red kangaroos, Macropus rufus (n = 150). Total milk solids increased from 11% at 0-40 days to 26% at permanent emergence from the pouch (235 days), then decreased towards weaning. Compared with other macropodids, milk from red kangaroos is relatively dilute. Carbohydrate concentrations increased from 2.0 to 6.2% at about Day 235 then declined while lipid concentrations increased from 3.9 to 10.3% over the course of lactation. Protein values increased from 5.0 to 7.0% prior to pouch emergence. Whey proteins were separated by means of SDS PAGE, identifying and confirming the presence of several phase-specific proteins. These results are similar to those reported for components of milk in captive red kangaroos and therefore confirm the general macropodid pattern of changing milk composition throughout lactation for a field population of red kangaroos.

scholarly journals CHANGES IN GENE EXPRESSION ASSOCIATED WITH CHILLING-UNIT ACCUMULATION IN DIFFERENT SPECIES OF BLUEBERRY

HortScience ◽  
1992 ◽  
Vol 27 (6) ◽  
pp. 580f-580 ◽  
Author(s):  
Lisa J. Rowland ◽  
M. Muthalif ◽  
Keyword(s):  
Gene Expression ◽  
Plant Species ◽  
Woody Plants ◽  
Molecular Weights ◽  
Sds Page ◽  
Specific Proteins

There is evidence from several plant species that low, nonfreezing temperatures induce the accumulation of specific proteins in leaves and stems. Only recently, however, have attempts been made to identify changes in gene expression in dormant buds of woody plants in response to chilling. For our investigations, we have used dormant blueberry plants representing three different species, placed them in a room maintained at about 4C, and collected buds after 0, 500, 1000, and 1500 hours. Proteins were extracted from bud samples and analyzed by SDS-PAGE. Results indicated that various cultvars and species responded differently to chilling unit accumulation. The most dramatic changes were noted in the V. corymbosum cultivar `Bluecrop'. The concentration of about 6 polypeptides with molecular weights ranging from 60-115 kD increased by 500 hours. The concentration of a 17.5 kD polypeptide increased after 1000 hours and the concentration of a 114 kD polypeptide decreased throughout the treatment.

scholarly journals Bark storage Protein in Peach, Plum, and Cherry Trees

HortScience ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 756A-756
Author(s):  
M.P. Bañados ◽  
M.S. Santiago ◽  
C. Eterovic
Keyword(s):  
Amino Acids ◽  
Storage Proteins ◽  
Protein Pattern ◽  
Fruit Trees ◽  
Sds Page ◽  
Bark Storage Proteins ◽  
Specific Proteins ◽  
Main Protein ◽  
Bark Storage Protein ◽  
Cherry Trees

The main form of nitrogen reserves during overwintering are amino acids and proteins. Specific proteins called bark storage proteins (BSP) have been characterized in many tree species. To identify BSPs in `O'Henry' peach, `Angeleno' plum, and `Early Burlat' cherry trees, samples of bark were collected from January through December 1993 from trees growing under field conditions in Santiago, Chile. SDS-PAGE analyses were used to characterize the seasonal variation on the protein pattern on the bark of those Prunus species. A 60 kDa BSP was identified in the bark of all three species, which corresponds to the main protein present in the bark during the winter. This protein may play an important role as a nitrogen reserve in these fruit trees.

scholarly journals Comparative proteome and metabolome analyses of latex-exuding and non-exuding Taraxacum koksaghyz roots provide insights into laticifer biology

2019 ◽  
Vol 71 (4) ◽  
pp. 1278-1293
Author(s):  
Vincent Alexander Benninghaus ◽  
Nicole van Deenen ◽  
Boje Müller ◽  
Kai-Uwe Roelfs ◽  
Ines Lassowskat ◽  
...  
Keyword(s):  
Physiological Role ◽  
Cell Types ◽  
Rna Degradation ◽  
Arbitrary Distribution ◽  
High Quality ◽  
Promising Alternative ◽  
Physiological Processes ◽  
Plant Environment ◽  
Entire Plant ◽  
Specific Proteins

Abstract Taraxacum koksaghyz has been identified as one of the most promising alternative rubber crops. Its high-quality rubber is produced in the latex of laticifers, a specialized cell type that is organized in a network of elongated tubules throughout the entire plant body. In order to gain insights into the physiological role(s) of latex and hence laticifer biology, we examine the effects of barnase-induced latex RNA degradation on the metabolite and protein compositions in the roots. We established high-quality datasets that enabled precise discrimination between cellular and physiological processes in laticifers and non-laticifer cell types of roots at different vegetative stages. We identified numerous latex-specific proteins, including a perilipin-like protein that has not been studied in plants yet. The barnase-expressing plants revealed a phenotype that did not exude latex, which may provide a valuable genetic basis for future studies of plant–environment interactions concerning latex and also help to clarify the evolution and arbitrary distribution of latex throughout the plant kingdom. The overview of temporal changes in composition and protein abundance provided by our data opens the way for a deeper understanding of the molecular interactions, reactions, and network relationships that underlie the different metabolic pathways in the roots of this potential rubber crop.

Еffect of different breeds on the protein profile in ram seminal plasma

2021 ◽  
Vol 24 (3) ◽  
pp. 344-354
Author(s):  
M. Ivanova ◽  
D. Gradinarska ◽  
S. Yotov ◽  
D. Abadjieva ◽  
Ts. Tzvetkov ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Biological Marker ◽  
Sds Page ◽  
Specific Proteins ◽  
Molecular Masses ◽  
Seminal Plasma Proteins ◽  
The Individual ◽  
Individual Profiles

In this study the individual profiles of seminal plasma proteins (SPP) in rams of three breeds – Merino, Pleven Blackhead and Ile de France - were analysed. The study was carried out with three rams at 3, 6 and 10 years of age, grown and fed under similar conditions. Eighteen ejaculates (6 ejaculates from each ram) were evaluated by Sperm Class Analyzer. The total SPP concentration was measured spectrophotometrically. The separation and characterisation of SPP was performed by HPLC and one dimensional polyacrylamide gel electrophoresis (SDS-PAGE). There were no significant differences between the characteristics of ejaculates and the main kinematic parameters of the sperm in the breeds studied. Chromatograms showed specific profiles with 9, 10 and 11 protein peaks for Merino, Pleven Blackhead and Ile de France breeds, respectively. The total SPP concentration was the highest in the Pleven Blackhead breed and the lowest in Ile de France breed. The major parts of SPP in the three breeds were identical. The seminal plasma of Merino breed contained proteins with molecular mass of 30.3 kDa, 15.7 kDa and 15.2 kDa that were not present in the other two breeds. In the Ile de France and Pleven Blackhead samples only, two proteins with molecular masses of 39.7 kDa and 21.1 kDa, were observed. In conclusion, the detection of specific proteins can be used as a biological marker for sheep breed identification.

scholarly journals Physical evaluation, morphological and identification of seminal proteins in Santa Ines sheep

2017 ◽  
Vol 18 (1) ◽  
pp. 211-220
Author(s):  
Marilza Assunção de OLIVEIRA ◽  
Roseane Pinto Martins de OLIVEIRA ◽  
Ana Rita de LIMA ◽  
Edmar Vaz de ANDRADE ◽  
Jan Sidarta Lima de ABREU ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Markers ◽  
Seminal Plasma ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Physiological Processes ◽  
Zeta Chain ◽  
Sds Page ◽  
Santa Inês ◽  
Dimensional Electrophoresis

SUMMARY This study aimed to identify proteins in the seminal plasma associated with fertility in sheep of Santa Inês in Manaus, AM, using twodimensional electrophoresis techniques associated with mass spectrometry. Semen samples from eight adult sheep were collected by removing an aliquot for the physical and morphological assessments of semen and seminal plasma was subjected to SDS-PAGE profile and two-dimensional electrophoresis. Gels were stained with colloidal Coomassie, scanned and analyzed using ImageMaster 2D Platinum software, version 6.0. The selected individual spots were cut from the master gel, digested with trypsin and subjected to identification by mass spectrometry (MALDITof / Tof). Of the 108 spots detected in the gel, it selected 10 differential spots (based on the distribution thereof in the bidimensional gel and pre-analysis of the 2D ImageMaster Platinum Software) identifying 03 proteins: clusterin, a protein 14-3-3 zeta chain and Ram Seminal versicles 22kDa Protein. The identity of these proteins implies that the components of seminal plasma participate in physiological processes involved in sperm protection, motility and sperm capacitation, all associated with fertility. These proteins need to be better studied to see whether the same could be used as molecular markers of fertility as they were also found in other studies conducted with sheep Santa Ines.

Identification of chicken (Gallus domesticus) adipocyte plasma membrane and differentiation specific proteins using SDS-page and western blotting

1992 ◽  
Vol 101 (1-2) ◽  
pp. 147-151 ◽  
Author(s):  
S.C. Butterwith ◽  
S. Kestin ◽  
H.D. Griffin ◽  
J. Beattie ◽  
D.J. Flint
Keyword(s):  
Plasma Membrane ◽  
Western Blotting ◽  
Gallus Domesticus ◽  
Sds Page ◽  
Specific Proteins
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