scholarly journals Inter-Specific Variation Studies among Nephrolepis using SDS-PAGE

2016 ◽  
Vol 2 (1) ◽  
Author(s):  
Johnson M
Keyword(s):  
Sds Page ◽  
Specific Variation

Proteomics Variation in Nigella Sativa L. (Rananculaceae) Germplasm

2021 ◽  
Vol 50 (2) ◽  
pp. 289-294
Author(s):  
Muhammad Sajjad Iqbal ◽  
Abdul Ghafoor
Keyword(s):  
Euclidean Distance ◽  
Nigella Sativa ◽  
Crop Improvement ◽  
Band Formation ◽  
First Report ◽  
Sds Page ◽  
Genetic Pattern ◽  
Specific Variation ◽  
Improvement Programs ◽  
Single Seeds

Study revealed a first report of proteomics variation in Nigella sativa L. based on analyzing 32 accessions through SDS-PAGE. Three prominent regions along eight subunits were identified. Intra specific variation was observed low whereas the sharpness of bands was high between first and second regions. It was noted that in second region there was no clear evidence of band formation in N. sativa. Prominent and sharp protein peptide bands were recorded in four accessions, namely PK-020561, PK-020609, PK-020620 and PK-020646. Further investigation of single seeds showed almost similar genetic pattern within the single accession. Five clusters were formed on the basis of Euclidean distance. Cluster-I & II contain 1, 1 accession each, likewise Cluster-III and C-IV contain 2, 2 accessions whereas Cluster-V was found diversified as consisted of 26 accessions. Two accessions PK-020878 and PK-020877 were recommended for polymorphism and crop improvement programs. Bangladesh J. Bot. 50(2): 289-294, 2021 (June)

scholarly journals ntra-species profiling of Cleome viscosa growing in Swat district (Pakistan)

2018 ◽  
Vol 26 (1) ◽  
pp. 52-55
Author(s):  
N. Muhammad ◽  
S. F. Wadood ◽  
W. Khan ◽  
N. Ali ◽  
M. Nisar
Keyword(s):  
Allelic Variation ◽  
Lower Surface ◽  
Protein Profiling ◽  
Yellow Colour ◽  
As Species ◽  
Sds Page ◽  
Specific Variation ◽  
Species Specific ◽  
High Level ◽  
Cleome Viscosa

Intra-specific genetic variation was studied in 28 genotypes of Cleome viscosa L. growing in Swat district, Khyber Pakhtunkhwa, Pakistan. It was found that genotypes showed the utmost allelic variation for leaf upper and lower surface with emerald green (75%), and yellow green (75%) respectively, other leaves lower and upper surfaces were (25%) green and yellow green (26%) respectively. The majority of C. viscosa genotypes were (50%) yellow flowers while others were with (29%) white yellow colour and (21%) dull yellow. Most of the seeds were with black (46%). The protein profiling was carried out on 12% gel electrophoresis; seven reproducible bands with molecular weight ranges from 180 to 10 KDa were detected in C. viscosa, the locus contribution toward genetic disagreement (LCTGD) of C. viscosa was 57%. Notably, L-3, L-4 L-5, was monomorphic in C. viscosa and was treated as species specific. L-1, L-2, L-7 were polymorphic. These bands showed 79%, 4%, 14% and 79% variation respectively. In the current investigation the intra-specific variation was observed limited and alone SDS-PAGE did not determine the high level of intra-specific variation; however, diverse germplasm were suggested to be acquired from various sources.

Inter and Intra-Specific Variation in SDS-PAGE of Total Seed Protein in Rice (Oryza sativa L.) Germplasm

2004 ◽  
Vol 7 (2) ◽  
pp. 139-143 ◽  
Author(s):  
Rehana Asghar ◽  
Rabia Siddique . ◽  
Muhammad Afzal . ◽  
Shamim Akhtar .
Keyword(s):  
Oryza Sativa ◽  
Seed Protein ◽  
Oryza Sativa L ◽  
Sds Page ◽  
Specific Variation ◽  
Total Seed

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.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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