SDS-PAGE analysis of the soluble leaf proteins in tomato inoculated with Xanthomonas campestris pv. vesicatoria

1989 ◽  
Vol 144 (8) ◽  
pp. 559-562 ◽  
Author(s):  
Mahendra Prasad ◽  
Jyoti Kumar
Keyword(s):  
Xanthomonas Campestris ◽  
Leaf Proteins ◽  
Sds Page

scholarly journals SDS-PAGE Characterisation of Crude Seed and Leaf Proteins in Corchorus Species

2015 ◽  
Vol 7 (2) ◽  
Author(s):  
Christiana Adeyinka AJALA ◽  
Joseph Akintade MORAKINYO
Keyword(s):  
Leaf Proteins ◽  
Sds Page

scholarly journals SDS-PAGE Characterisation of Crude Seed and Leaf Proteins in Corchorus Species

2015 ◽  
Vol 7 (2) ◽  
pp. 177-183
Author(s):  
Christiana Adeyinka AJALA ◽  
Joseph Akintade MORAKINYO
Keyword(s):  
Protein Separation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Study ◽  
Single Linkage ◽  
Banding Patterns ◽  
Leaf Proteins ◽  
Sds Page ◽  
Single Linkage Cluster ◽  
Linkage Cluster

Crude protein separation was carried out for Corchorus incisifolious, Corchorus aestuans, Corchorus tridens and Corchorus olitorious using Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). Plants were collected both from wild and cultivated sites and samples included leaves and seeds for the electrophoretic study. Distinct polymorphism in electrophoretic banding patterns of seed and leaf proteins following SDS- PAGE was observed in the four Corchorus species studied. Forty- two polypeptide bands were observed in the seed and a total of eleven polypeptide bands were observed in the leaves of the Corchorus species studied. The electrophoretic study revealed protein bands with various intensities ranging from high, to low and faint. The results showed that there was variation in both the seed and leaf proteins of the Corchorus species studied. A dendrogram constructed based on the Single Linkage Cluster Analysis (SLCA) clustering method revealed three major clusters for seeds. Cluster I consisted of C. incisifolious and C. aestuans, cluster II consisted of C. tridens, while cluster III consisted of C. olitorious. The leaf protein extracts were grouped into two clusters, cluster one containing C. incisifolious and C. aestuans, while the other contained C. tridens and C. olitorious.

scholarly journals Induction of Extracellular Matrix Glycoproteins in Brassica Petioles by Wounding and in Response to Xanthomonas campestris

1997 ◽  
Vol 10 (7) ◽  
pp. 812-820 ◽  
Author(s):  
Huw A. Davies ◽  
Michael J. Daniels ◽  
J. Maxwell Dow
Keyword(s):  
Extracellular Matrix ◽  
Xanthomonas Campestris ◽  
Brassica Campestris ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Virulent Strains ◽  
Sds Page ◽  
Number Of Genes ◽  
Microbe Interactions

A panel of monoclonal antibodies that recognize plant extracellular matrix glycoproteins previously implicated in plant-microbe interactions was used to study the effects of pathogen inoculation and wounding on glycoproteins in petioles of Brassica campestris. The panel of monoclonals comprised two sets: JIM11, JIM12, and JIM20 recognize epitopes carried on hydroxyproline-rich glycoproteins (HRGPs) (M. Smallwood, A. Beven, N. Donovan, S. J. Neill, J. Peart, K. Roberts, and J. P. Knox, Plant J. 5:237–246, 1994); MAC204 and MAC265 recognize glycoproteins of the Rhizobium infection thread (K. A. VandenBosch, D. J. Bradley, S. Perotto, G. W. Butcher, and N. J. Brewin, EMBO J. 8:335–342, 1989). Wounding or inoculation of petioles with avirulent strains of pathovars of Xanthomonas campestris induced the synthesis of two new groups of antigens: gp160 ran as a smear on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with apparent molecular mass from 120 to 200 kDa and was recognized by JIM20 and MAC204; gpS remained in the stacking gel on SDS-PAGE and was recognized by JIM11, JIM20, and MAC204. The response to virulent strains of pathovars of X. campestris was either less pronounced or absent. gpS comprised several components that were resolved by cation-exchange chromatography. Some of these components were characterized as extensin-like HRGPs. The level of induction of the gpS group of antigens by virulent strains was not altered by mutation of a number of genes required for basic pathogenicity or by heat-killing the bacteria.

scholarly journals Grouping of Xanthomonas campestris pathovars by SDS-PAGE of proteins

1991 ◽  
Vol 137 (7) ◽  
pp. 1677-1687 ◽  
Author(s):  
L. Vauterin ◽  
J. Swings ◽  
K. Kersters
Keyword(s):  
Xanthomonas Campestris ◽  
Sds Page

3-D organization of fibrinogen receptors using computer reconstruction and whole-mount microscopy

1988 ◽  
Vol 46 ◽  
pp. 30-31
Author(s):  
E. T. O'Toole ◽  
R. R. Hantgan ◽  
J. C. Lewis
Keyword(s):  
Whole Blood ◽  
Colloidal Gold ◽  
Blood Platelets ◽  
Cell Contact ◽  
Computer Assisted ◽  
Adherent Cells ◽  
Differential Centrifugation ◽  
Computer Reconstruction ◽  
Sds Page ◽  
Whole Mount

Thrombocytes (TC), the avian equivalent of blood platelets, support hemostasis by aggregating at sites of injury. Studies in our lab suggested that fibrinogen (fib) is a requisite cofactor for TC aggregation but operates by an undefined mechanism. To study the interaction of fib with TC and to identify fib receptors on cells, fib was purified from pigeon plasma, conjugated to colloidal gold and used both to facilitate aggregation and as a receptor probe. Described is the application of computer assisted reconstruction and stereo whole mount microscopy to visualize the 3-D organization of fib receptors at sites of cell contact in TC aggregates and on adherent cells.Pigeon TC were obtained from citrated whole blood by differential centrifugation, washed with Ca++ free Hank's balanced salts containing 0.3% EDTA (pH 6.5) and resuspended in Ca++ free Hank's. Pigeon fib was isolated by precipitation with PEG-1000 and the purity assessed by SDS-PAGE. Fib was conjugated to 25nm colloidal gold by vortexing and the conjugates used as the ligand to identify fib receptors.

Parallel Reduction of Plasma Levels of High and Low Molecular Weight Kininogen in Patients with Cirrhosis

1999 ◽  
Vol 82 (11) ◽  
pp. 1428-1432 ◽  
Author(s):  
Cheryl Scott ◽  
Francesco Salerno ◽  
Elettra Lorenzano ◽  
Werner Müller-Esterl ◽  
Angelo Agostoni ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Liver Disease ◽  
Liver Function ◽  
Plasma Levels ◽  
Plasma Concentrations ◽  
Normal Subjects ◽  
Low Molecular Weight ◽  
Major Band ◽  
Sds Page ◽  
Normal Controls

SummaryLittle is known about the regulation of high-molecular-weight-kininogen (HK) and low-molecular-weight-kininogen (LK) or the relationship of each to the degree of liver function impairment in patients with cirrhosis. In this study, we evaluated HK and LK quantitatively by a recently described particle concentration fluorescence immunoassay (PCFIA) and qualitatively by SDS PAGE and immunoblotting analyses in plasma from 33 patients with cirrhosis presenting various degrees of impairment of liver function. Thirty-three healthy subjects served as normal controls. Patients with cirrhosis had significantly lower plasma levels of HK (median 49 μg/ml [range 22-99 μg/ml]) and LK (58 μg/ml [15-100 μg/ml]) than normal subjects (HK 83 μg/ml [65-115 μg/ml]; LK 80 μg/ml [45-120 μg/ml]) (p < 0.0001). The plasma concentrations of HK and LK were directly related to plasma levels of cholinesterase (P < 0.0001) and albumin (P < 0.0001 and P < 0.001) and inversely to the Child-Pugh score (P < 0.0001) and to prothrombin time ratio (P < 0.0001) (reflecting the clinical and laboratory abnormalities in liver disease). Similar to normal individuals, in patients with cirrhosis, plasma HK and LK levels paralleled one another, suggesting that a coordinate regulation of those proteins persists in liver disease. SDS PAGE and immunoblotting analyses of kininogens in cirrhotic plasma showed a pattern similar to that observed in normal controls for LK (a single band at 66 kDa) with some lower molecular weight forms noted in cirrhotic plasma. A slight increase of cleavage of HK (a major band at 130 kDa and a faint but increased band at 107 kDa) was evident. The increased cleavage of HK was confirmed by the lower cleaved kininogen index (CKI), as compared to normal controls. These data suggest a defect in hepatic synthesis as well as increased destructive cleavage of both kininogens in plasma from patients with cirrhosis. The decrease of important regulatory proteins like kininogens may contribute to the imbalance in coagulation and fibrinolytic systems, which frequently occurs in cirrhotic patients.

The Anticoagulant Properties of a Modified Form of Protein S

1988 ◽  
Vol 60 (02) ◽  
pp. 298-304 ◽  
Author(s):  
C A Mitchell ◽  
S M Kelemen ◽  
H H Salem
Keyword(s):  
Monoclonal Antibody ◽  
Anticoagulant Activity ◽  
Activated Protein C ◽  
Factor Xa ◽  
Protein S ◽  
Human Neutrophil Elastase ◽  
Factor X ◽  
Sds Page

SummaryProtein S (PS) is a vitamin K-dependent anticoagulant that acts as a cofactor to activated protein C (APC). To date PS has not been shown to possess anticoagulant activity in the absence of APC.In this study, we have developed monoclonal antibody to protein S and used to purify the protein to homogeneity from plasma. Affinity purified protein S (PSM), although identical to the conventionally purified protein as judged by SDS-PAGE, had significant anticoagulant activity in the absence of APC when measured in a factor Xa recalcification time. Using SDS-PAGE we have demonstrated that prothrombin cleavage by factor X awas inhibited in the presence of PSM. Kinetic analysis of the reaction revealed that PSM competitively inhibited factor X amediated cleavage of prothrombin. PS preincubated with the monoclonal antibody, acquired similar anticoagulant properties. These results suggest that the interaction of the monoclonal antibody with PS results in an alteration in the protein exposing sites that mediate the observed anticoagulant effect. Support that the protein was altered was derived from the observation that PSM was eight fold more sensitive to cleavage by thrombin and human neutrophil elastase than conventionally purified protein S.These observations suggest that PS can be modified in vitro to a protein with APC-independent anticoagulant activity and raise the possibility that a similar alteration could occur in vivo through the binding protein S to a cellular or plasma protein.

Sign in / Sign up

Export Citation Format

Share Document