An evaluation of the polyacrylamide gel electrophoresis fractionation method for the production of Mycobacterium tuberculosis skin test preparations II. Comparative skin testing on guinea-pigs

1986 ◽  
Vol 14 (3) ◽  
pp. 187-200 ◽  
Author(s):  
L.F. Affronti ◽  
M.W. Bentzon ◽  
A. Lind ◽  
M. Magnusson ◽  
Ö. Ouchterlony ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Skin Test ◽  
Gel Electrophoresis ◽  
Guinea Pigs ◽  
Skin Testing ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Fractionation Method ◽  
Tuberculosis Skin Test

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

1979 ◽  
Author(s):  
C Cierniewski ◽  
T Krajewski ◽  
E Janiak
Keyword(s):  
Gel Electrophoresis ◽  
Functional Relationship ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Functional Similarity ◽  
Fractionation Method ◽  
Relationship Of ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule ◽  
Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

1979 ◽  
Author(s):  
C.S. Ciernlewski ◽  
T. Krajewski ◽  
E. Janiak
Keyword(s):  
Gel Electrophoresis ◽  
Functional Relationship ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Functional Similarity ◽  
Fractionation Method ◽  
Relationship Of ◽  
Fibrin Monomers ◽  
Fibrinogen Molecule ◽  
Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerisation sites In the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces, Amphibia, Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces, Amphibia, Ayes and Mammalia interacted in a specific way with Immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS Polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

scholarly journals Protein extraction method of Metroxylon sagu leaf for high resolution two dimensional gel electrophoresis and comparative proteomics

2019 ◽  
Author(s):  
Mehvish Nisar ◽  
Hasnain Hussain
Keyword(s):  
Gel Electrophoresis ◽  
Extraction Method ◽  
Protein Extraction ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Fractionation Method ◽  
Metroxylon Sagu ◽  
Time Required

Abstract Objective This study aimed to determine the best protein extraction method of Metroxylon sagu for the two-dimensional gel electrophoresis and the comparative analysis. Results To perform good proteome research, the most critical step is to establish a method that gives the best quality of extracted total proteins. To develop an optimized protein extraction protocol for two-dimensional polyacrylamide gel electrophoresis (2-DE) analysis of Metroxylon sagu, five protein extraction protocols were compared; polyethene glycol (PEG) fractionation method, SDS/phenol method, TCA/acetone method, combination SDS/phenol and TCA/acetone and imidazole method. The PEG fractionation method was found to give the most reproducible gels with the highest number of spots and highest protein concentration followed by SDS/Phenol method. The lowest number of spots were observed in Imidazole method. The PEG fractionation method provides improved resolution and reproducibility of two-dimensional polyacrylamide gel electrophoresis (2-DE) and reduces the time required to analyze samples. Partitioning rubisco by polyethene glycol (PEG) fractionation provides clearer detection of low-abundance protein. Hence the result from this study propose PEG fractionation as the effective protein extraction method for 2-DE proteomic studies of Metroxylon sagu.

scholarly journals Protein extraction method of Metroxylon sagu leaf for high resolution two dimensional gel electrophoresis and comparative proteomics

2019 ◽  
Author(s):  
Mehvish Nisar ◽  
Hasnain Hussain
Keyword(s):  
Gel Electrophoresis ◽  
Extraction Method ◽  
Protein Extraction ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Fractionation Method ◽  
Metroxylon Sagu ◽  
Time Required

Abstract Objective This study aimed to determine the best protein extraction method of Metroxylon sagu for the two-dimensional gel electrophoresis and the comparative analysis. Results To perform good proteome research, the most critical step is to establish a method that gives the best quality of extracted total proteins. To develop an optimized protein extraction protocol for two-dimensional polyacrylamide gel electrophoresis (2-DE) analysis of Metroxylon sagu, five protein extraction protocols were compared; polyethene glycol (PEG) fractionation method, SDS/phenol method, TCA/acetone method, combination SDS/phenol and TCA/acetone and imidazole method. The PEG fractionation method was found to give the most reproducible gels with the highest number of spots and highest protein concentration followed by SDS/Phenol method. The lowest number of spots were observed in Imidazole method. The PEG fractionation method provides improved resolution and reproducibility of two-dimensional polyacrylamide gel electrophoresis (2-DE) and reduces the time required to analyze samples. Partitioning rubisco by polyethene glycol (PEG) fractionation provides clearer detection of low-abundance protein. Hence the result from this study propose PEG fractionation as the effective protein extraction method for 2-DE proteomic studies of Metroxylon sagu.

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

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