Differences in the biochemical compositions and elicitor activity of extracellular components produced by three races of a fungal plant pathogen, Colletotrichum lindemuthianum

1980 ◽  
Vol 26 (12) ◽  
pp. 1473-1479 ◽  
Author(s):  
Aaanne J. Anderson
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Colletotrichum Lindemuthianum ◽  
Neutral Sugar ◽  
Sugar Composition ◽  
Fungal Plant Pathogen ◽  
Red Kidney Bean ◽  
Weakly Virulent ◽  
Protein Components ◽  
Highly Virulent

High molecular weight products from the α, β, and γ races of Colletotrichum lin-differed in their carbohydrate and protein compositions and in their abilities to elicit symptoms of a hypersensitive response in dark red kidney bean. The neutral sugar composition of the products varied in their proportions of rhamnose, mannose, galactose, and glucose. Polyacrylamide gel electrophoresis showed the protein components to be more numerous in the β race products than in the α or γ race products. Each protein band co-stained for carbohydrate. Highest elicitor activity was observed in the products from the α race, a race avirulent on dark red kidney. The products from the weakly virulent γ race were about 10-fold less active as elicitors than those of the α race. With the β race, a race highly virulent on dark red kidney, elicitor activity was 100-fold less than that of the α race.

scholarly journals Weissellicin 110, a Newly Discovered Bacteriocin from Weissella cibaria 110, Isolated from Plaa-Som, a Fermented Fish Product from Thailand

2007 ◽  
Vol 73 (7) ◽  
pp. 2247-2250 ◽  
Author(s):  
Sirinat Srionnual ◽  
Fujitoshi Yanagida ◽  
Li-Hsiu Lin ◽  
Kuang-Nan Hsiao ◽  
Yi-sheng Chen
Keyword(s):  
Proteolytic Enzymes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Band ◽  
Proteinase K ◽  
Mass Spectrometry Analysis ◽  
Fermented Fish ◽  
Spectrometry Analysis ◽  
Weissella Cibaria ◽  
Fish Product

ABSTRACT Weissella cibaria 110, isolated from the Thai fermented fish product plaa-som, was found to produce a bacteriocin active against some gram-positive bacteria. Bacteriocin activity was not eliminated by exposure to high temperatures or catalase but was destroyed by exposure to the proteolytic enzymes proteinase K and trypsin. The bacteriocin from W. cibaria 110 was purified, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the purified bacteriocin contained one protein band that was approximately 2.5 kDa in size. Mass spectrometry analysis showed the mass of the peptide to be approximately 3,487.8 Da. N-terminal amino acid sequence analysis was performed, and 27 amino acids were identified. Because it has no similarity to other known bacteriocins, this bacteriocin was defined as a new bacteriocin and termed weissellicin 110.

scholarly journals Evaluation of SDS-Polyacrylamide gel electrophoresis and immunostrip technique for detection of Tobacco mosaic virus and Cucumber mosaic virus in IRAQ

2011 ◽  
Vol 5 (2) ◽  
pp. 85-94
Author(s):  
Rakib A. Al-Ani ◽  
Mustafa A. Adhab
Keyword(s):  
Tobacco Mosaic Virus ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Positive Reaction ◽  
Total Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Polyacrylamide Gel ◽  
Total Proteins ◽  
Winter Squash

his study was carried out to evaluate the efficiency of electrophoresis on SDS- poly acrylamide slap gel and immunostrip techniques for detection of Tobacco mosaic virus (TMV, genus Tobamovirus) and Cucumber mosaic virus (CMV, genus Cucumovirus, family Bromoviridae), compared with symptoms on diagnostic plants for the two viruses. The results obtained showed that the two methods were effective. The analysis of samples of purified CMV, total proteins from infected cucumber plants, and extracts from infected plants with or without chlorophyll, by electrophoresis on 10% polyacrylamide slap gel containing 0.1% SDS showed two bands of 24 and 26 kd in size, and absent in samples of total protein or extracts of healthy plants. These two proteins represent the coat protein (CP) of CMV. In addition, one 18 kd protein band appeared on SDS- polyacrylamide gel profile which represent the CP of TMV, when samples of purified virus, total protein of infected plants, and plant extracts with or without chlorophyll were analyzed. This band was absent in similar samples from healthy plants. The test of immunostrip specific for CMV showed positive reaction with extracts from melon, cucumber, winter squash, and zucchini infected plants. Similarly, a positive reaction with immunostrip specific for TMV appeared with extracts from tobacco, tomato infected with TMV. No reaction was obtained with healthy plants extract. These results were similar to those obtained from indicator plants for the two viruses.

Thrombin-Induced Surface Changes of Human Platelets in Plasma: Their Relation to Serotonin Release

1979 ◽  
Author(s):  
K. Subbarao ◽  
V.V. Kakkar
Keyword(s):  
Membrane Proteins ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Human Platelets ◽  
Serotonin Release ◽  
Glycoprotein I ◽  
Reversible Aggregation ◽  
Coomassie Blue ◽  
Labeling Pattern

Membrane proteins of both control and thrombin-treated platelets were labeled by NaB3H4, reduction of Schiff bases formed between pyridoxal 5′-phosphate and protein amino groups. Examination of the labeled polypeptides by SDS-polyacrylamide gel electrophoresis and fluorography disclosed a different labeling pattern for thrombin-treated platelets. The distributions of Coomassie blue-stained protein from treated and untreated cells were, by contrast, almost identical. Fluorographs of control platelets showed a single intensely labeled protein band (mol wt 90,000) whereas with cells exposed to thrombin (30-60 milliunits) about 10 protein bands with mol wts ranging from 43,000 to 200,000 were typically present. Among these were: thrombin-sensitive protein (mol wt 188,000), glycoprotein I (mol wt 150,000) and actin (mol wt 43,000). When serotonin release was prevented, either by reversing platelet aggregation with low amounts of ADP (0.1-0.3 μM) or by preincubating with 3',5'-ADP (20 μM), an inhibitor of both ADP- and thrombin-induced platelet function, the labeling patterns on fluorographs were similar to the control. These results indicate that blood platelets can undergo reversible aggregation without major changes in their surface topography, whereas thrombin-induced serotonin release appears related to structural alterations in platelet membrane proteins.

scholarly journals Changes in cell wall neutral sugar composition related to pectinolytic enzyme activities and intra-flesh textural property during ripening of ten apricot clones

2021 ◽  
Vol 339 ◽  
pp. 128096
Author(s):  
Jamal Ayour ◽  
Carine Le Bourvellec ◽  
Barbara Gouble ◽  
Jean-Marc Audergon ◽  
Mohamed Benichou ◽  
...  
Keyword(s):  
Cell Wall ◽  
Enzyme Activities ◽  
Neutral Sugar ◽  
Textural Property ◽  
Sugar Composition ◽  
Pectinolytic Enzyme

Three new components contained in the vitelline coat of Tegula pfeifferi

Zygote ◽  
1999 ◽  
Vol 8 (S1) ◽  
pp. S61-S61 ◽  
Author(s):  
Kazu Haino-Fukushima ◽  
Xuxi Fan ◽  
Shouka Nakamura
Keyword(s):  
Amino Acids ◽  
Polyacrylamide Gel Electrophoresis ◽  
Enzymatic Reaction ◽  
Base Pairs ◽  
Sulphated Polysaccharides ◽  
Reading Frame ◽  
Glycosylation Sites ◽  
Long Time ◽  
Protein Components ◽  
Vitelline Coat

The vitelline coat (VC) lysin of Tegula, a marine molluscan genus, is released from the acrosome of sperm during fertilisation and can lyse the VC of only the same species. The lytic action of this lysin against the VC is not an enzymatic reaction, but a stoichiometric and irreversible one (Haino-Fukushima, 1974).The VC of Tegula pfeifferi consists of glycoproteins containing sulphated polysaccharides, which account for roughly two-thirds of the entire weight of the VC. The presence of a large quantity of polysaccharides in the VC had prevented rapid progress in the analysis of its protein components. Last year, we succeeded in a complete solubilisation of the VC by boiling for a long time in 1% SDS solution, and determined the cDNA sequence coding for a mature 41 kDa glycoprotein, which appears to be the major component of the VC from the results of SDS-polyacrylamide gel electrophoresis (PAGE). The cDNA, referred to as vcp41, comprises 1072 base pairs and contains one open reading frame with a sequence for 319 amino acids containing 19 amino acids of a signal peptide. The deduced amino acid sequence has five N-glycosylation sites and ten cysteine residues. It seems that almost 7 kDa in this 41kDa glycoprotein is polysaccharide constituents (Fan & Haino-Fukushima, 1998).

scholarly journals Phaseolin type and heat treatment influence the biochemistry of protein digestion in the rat intestine

2008 ◽  
Vol 99 (3) ◽  
pp. 531-539 ◽  
Author(s):  
Carlos A. Montoya ◽  
Pascal Leterme ◽  
Stephen Beebe ◽  
Wolfgang B. Souffrant ◽  
Daniel Mollé ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Western Blotting ◽  
Sole Source ◽  
Protein Band ◽  
Molecular Weights ◽  
Endogenous Protein ◽  
Anionic Trypsin ◽  
Endogenous Proteins ◽  
Protein Components

The study aimed to investigate thein vivodigestion ofPhaseolus vulgarisphaseolin types differing in their subunit pattern composition. Diets contained either casein as the sole source of protein or a mixture (1:1) of casein and pure Sanilac (S), Tendergreen (T) or Inca (I) phaseolin either unheated or heated. Rats were fed for 11 d with the experimental diets. Their ileal content and mucosa were collected and prepared for electrophoresis, Western blotting, densitometry and MS. Differences in digestion among native phaseolin types were observed for intact phaseolin at molecular weights (MW) of 47–50·5 kDa and for an undigested fragment at MW of 19–21·5 kDa in ileal digesta. In both cases, the concentration of these protein bands was lower for I phaseolin than for S or T phaseolin (P < 0·05). In the mucosa, the concentration of a protein band at MW of 20·5–21·5 kDa was lower for S phaseolin as compared to T or I phaseolin (P < 0·001). The presence of phaseolin subunits and their fragments was confirmed by Western blotting. MS analysis revealed the presence of undigested α and β subunit fragments from phaseolin and endogenous proteins (anionic trypsin I and pancreatic α-amylase) in ileal digesta. Thermal treatment improved digestion (P < 0·01), acting on both dietary and endogenous protein components. In conclusion, this study provides evidence for differences in intestinal digestion among phaseolin types, S phaseolin being more resistant and I phaseolin more susceptible. These differences were affected by the origin of the phaseolin subunit precursor. Heat treatment enhanced phaseolin digestion.

Changes in grapefruit flavedo cell wall noncellulosic neutral sugar composition

1993 ◽  
Vol 34 (5) ◽  
pp. 1235-1239 ◽  
Author(s):  
Elizabeth J. Mitcham ◽  
Roy E. McDonald
Keyword(s):  
Cell Wall ◽  
Neutral Sugar ◽  
Sugar Composition

Two-dimensional electrophoretic analysis of erythrocyte membranes.

1982 ◽  
Vol 28 (4) ◽  
pp. 925-931 ◽  
Author(s):  
B B Rosenblum ◽  
S M Hanash ◽  
N Yew ◽  
J V Neel
Keyword(s):  
Erythrocyte Membrane ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Analysis ◽  
High Molecular Mass ◽  
Erythrocyte Membranes ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Protein Components ◽  
Erythrocyte Membrane Proteins ◽  
Dimensional Electrophoresis

Abstract In an effort to maximize the amount of genetic information that can be extracted from a blood sample, we investigated the use of two-dimensional polyacrylamide-gel electrophoresis (PAGE) to resolve the protein constituents of the erythrocyte membrane. Lyophilized membranes were dissolved in various concentrations of urea, NP-40 detergent, and mercaptoethanol and subjected to two-dimensional PAGE by a modification of the O'Farrell procedure, with use of the ISO-DALT apparatus. More than 600 spots were visible in silver-stained gels under conditions that excluded specific cytoskeleton protein components, including spectrin and actin. The reproducibility of the pattern depended highly on the precise composition of the solubilization mixture. Poor resolution was observed in the presence of actin and other proteins of high molecular mass (spectrin bands 1 and 2) when we used high urea concentrations that solubilized the entire erythrocyte membrane. The large number of polypeptides observed could not be attributed to proteolysis, because addition of proteolytic inhibitors to the membrane wash solutions did not alter the pattern on the gel. The pattern also did not appear to include erythrocyte cytosol proteins because, except for globin, none of five purified erythrocyte lysate proteins was visible in the erythrocyte membrane gels. We conclude that two-dimensional electrophoresis provides a powerful tool for the study of non-cytoskeletal erythrocyte membrane proteins.

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