Separation of proteins with a molecular mass difference of 2 kDa utilizing preparative double-inverted gradient polyacrylamide gel electrophoresis under nonreducing conditions: Application to the isolation of 24 kDa human growth hormone

2005 ◽  
Vol 26 (23) ◽  
pp. 4389-4395 ◽  
Author(s):  
Juan J. Bustamante ◽  
Macario Garcia ◽  
Leticia Gonzalez ◽  
Jesus Garcia ◽  
Rafael Flores ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Molecular Mass ◽  
Human Growth Hormone ◽  
Gel Electrophoresis ◽  
Mass Difference ◽  
Polyacrylamide Gel Electrophoresis ◽  
Human Growth ◽  
Polyacrylamide Gel ◽  
Separation Of Proteins

scholarly journals Polymorphism of Gli-D1 alleles of Kragujevac’s winter wheat cultivars (Triticum aestivum L.)

Genetika ◽  
2007 ◽  
Vol 39 (2) ◽  
pp. 273-282
Author(s):  
Desimir Knezevic ◽  
Aleksandra Novoselskaya-Dragovich
Keyword(s):  
Triticum Aestivum ◽  
Winter Wheat ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel ◽  
Wheat Cultivars ◽  
Number Of Components ◽  
Winter Wheat Cultivars

Composition of gliadins encoded by Gli-D1 allele as well polymorphisms of Gli-D1 allele investigated in 25 wheat cultivars by using acid polyacrylamide gel electrophoresis. Electrophoregrams obtained by polyacrylamide gel electrophoresis were used for estimation variability of gliadin components and identification of gliadin blocks. Five gliadin blocks encoded by different alleles at Gli-D1 locus were apparently expressed and identified. Gliadin blocks differed according to number of components and their molecular mass. Variability of determined block components indicates that existing polymorphisms of gliadins alleles. Frequency of identified 5 alleles at Gli-D1 locus was in ratio from 4% to 52%. The highest frequency of b allele and the of g allele was found.

scholarly journals The small dermatan sulphate proteoglycans synthesized by fibroblasts derived from skin, synovium and gingiva show tissue-related heterogeneity

1988 ◽  
Vol 256 (1) ◽  
pp. 35-40 ◽  
Author(s):  
H Larjava ◽  
J Heino ◽  
T Krusius ◽  
E Vuorio ◽  
M Tammi
Keyword(s):  
Extracellular Matrix ◽  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Core Protein ◽  
Culture Media ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Gingival Fibroblasts ◽  
Dermatan Sulphate ◽  
Different Tissues

Dermatan sulphate proteoglycans (DSPGs) synthesized in the presence of 35SO4 were characterized in culture media of fibroblast lines obtained from skin, synovium, and gingiva. The molecular mass of DSPG varied from 95-130 kDa as estimated by SDS/polyacrylamide-gel electrophoresis. Gingival fibroblasts constantly produced larger DSPGs than skin fibroblasts. This was due to the larger dermatan sulphate (DS) chains, which also showed tissue-related heterogeneity in the distribution of 4- and 6-sulphated disaccharide units. The N-glycosylated cores (44 and 47 kDa) obtained following chondroitinase ABC treatment were of identical size in all tissues. The cores from the different tissues were also of the same size (38 kDa) when addition of the N-linked oligosaccharides was inhibited by tunicamycin or when they were removed by N-glycanase treatment. No evidence for low-molecular-mass sulphated oligosaccharides was found. All tissues contained two mRNA species (1.6 and 1.9 kb) for the DSPG core protein. These data suggest that the pattern of transferase activities involved in the construction of DS chains differs from one tissue to another. This variation may modulate the functions of DSPG in the extracellular matrix.

Enhanced electrophoretic separation of proteins by tethered SiO2 nanoparticles in an SDS-polyacrylamide gel network

The Analyst ◽  
2020 ◽  
Vol 145 (2) ◽  
pp. 415-423 ◽  
Author(s):  
Sayyed Hashem Sajjadi ◽  
Hossein Ahmadzadeh ◽  
Elaheh K. Goharshadi
Keyword(s):  
Gel Electrophoresis ◽  
Heat Dissipation ◽  
Separation Efficiency ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sio2 Nanoparticles ◽  
Polyacrylamide Gel ◽  
Electrophoretic Separation ◽  
Sds Page ◽  
Separation Of Proteins ◽  
Gel Network

Tethered nanoparticles (NPs) are able to improve the separation efficiency of proteins in SDS-polyacrylamide gel electrophoresis (SDS-PAGE) due to their capability of enhancing heat dissipation during electrophoresis and restriction of electrophoretic movement of NPs.

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