Enhanced resolution in two-dimensional electrophoresis of low-molecular-weight proteins while utilizing enlarged gels

1982 ◽  
Vol 127 (2) ◽  
pp. 235-246 ◽  
Author(s):  
Ben F. Johnson
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Enhanced Resolution ◽  
Dimensional Electrophoresis ◽  
Low Molecular Weight Proteins

scholarly journals Changes in ribosomal proteins in wheat embryos in the course of grain development and maturation

2014 ◽  
Vol 51 (2) ◽  
pp. 283-290
Author(s):  
Stanisław Weidner ◽  
Kazimierz Zalewski
Keyword(s):  
Molecular Weight ◽  
Ribosomal Proteins ◽  
Low Molecular Weight ◽  
Two Dimensional ◽  
Grain Development ◽  
Two Dimensional Electrophoresis ◽  
Wheat Embryos ◽  
The Cost ◽  
Dimensional Electrophoresis ◽  
Low Molecular Weight Proteins

It was found, by comparing the densitometric profiles of ribosomal proteins of wheat embryos in milk and full grain ripeness, that in the process of development and ripening of caryopses the percentual proportion of low molecular weight proteins increases at the cost of those of high molecular weight. This concerns both acidic and basic proteins. In electrophoretic separation of ribosomal proteins from embryos of fully ripe seeds by the method of two-dimensional electrophoresis the appearance of three new low molecular weight proteins - an acidic one and two basic ones - was observed. These proteins were not found in the embryos of caryopses of milk ripeness. These results indicate that with development and ripening of wheat caryopses new low molecular weight ribosomal proteins are built into the ribosomes in the embryo. These changes are both quantitative and qualitative.

Detection of low-molecular weight allergens resolved on two-dimensional electrophoresis with acid–urea polyacrylamide gel

2006 ◽  
Vol 351 (2) ◽  
pp. 290-297 ◽  
Author(s):  
Kazumi Kitta ◽  
Mayumi Ohnishi-Kameyama ◽  
Tatsuya Moriyama ◽  
Tadashi Ogawa ◽  
Shinichi Kawamoto
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel ◽  
Low Molecular Weight ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Analysis of low molecular weight plasma proteins using ultrafiltration and large gel two-dimensional electrophoresis

PROTEOMICS ◽  
2009 ◽  
Vol 9 (7) ◽  
pp. 1827-1840 ◽  
Author(s):  
Woon-Won Jung ◽  
Sohee Phark ◽  
Sangnam Oh ◽  
Jin-Young Khim ◽  
Juneyoung Lee ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Plasma Proteins ◽  
Low Molecular Weight ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Chromosomal locations of the structural genes for secalins in wild perennial rye (Secale montanum Guss.) and cultivated rye (S. cereale L.) determined by two-dimensional electrophoresis

1986 ◽  
Vol 28 (1) ◽  
pp. 76-83 ◽  
Author(s):  
P. R. Shewry ◽  
S. Parmar ◽  
N. Fulrath ◽  
D. D. Kasarda ◽  
T. E. Miller
Keyword(s):  
Molecular Weight ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Relative Molecular Mass ◽  
Two Dimensional ◽  
Structural Genes ◽  
Substitution Lines ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Secale Montanum

The chromosomal locations of the structural genes for secalin storage proteins in Secale cereale and S. montanum were determined by electrophoresis of grain proteins from wheat–rye addition and substitution lines. The use of several different extraction procedures and high-resolution electrophoretic systems (one and two dimensional) enabled us to demonstrate that the genes for all the high molecular weight secalins are present on chromosome IRL, and for all the ω-secalins and at least some of the γ-secalins with a relative molecular mass (Mr) of 40 000 on chromosome IRS of both species. In contrast, the genes for the γ-secalins (Mr = 75 000) are located on 2RcS in S. cereale but 6Rm in S. montanum. These observations are discussed in relation to evolution of prolamins and their genes in Secale and related members of the Triticeae.Key words: Secale, rye, seed proteins, structural genes, two-dimensional electrophoresis.

scholarly journals Two-dimensional Electrophoresis of High Molecular Weight Glutenin Subunits in Korean Wheat Cultivars

2013 ◽  
Vol 45 (3) ◽  
pp. 240-252 ◽  
Author(s):  
Jong-Yeol Lee ◽  
Chul-Soo Park ◽  
Hyo-Jung Kim ◽  
Joo-Hyung Kim ◽  
Min-Suk Kim ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Two Dimensional ◽  
Wheat Cultivars ◽  
Glutenin Subunits ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

The oral apparatus of Tetrahymena. V. Oral apparatus polypeptides and their distribution

1980 ◽  
Vol 44 (1) ◽  
pp. 317-333
Author(s):  
R.H. Gavin
Keyword(s):  
Molecular Weight ◽  
Basal Body ◽  
Tetrahymena Thermophila ◽  
Electrophoretic Analysis ◽  
Two Dimensional ◽  
Molecular Weight Range ◽  
Two Dimensional Electrophoresis ◽  
Weight Range ◽  
Isoelectric Points ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis was used to resolve approximately 162 polypeptides from the isolated oral apparatus of Tetrahymena thermophila. The molecular weight range was between 110 000 and 15 000 Daltons. The polypeptides had apparent isoelectric points between pH 3.3 and pH 7.2. Electrophoretic analysis of isolated ciliary axonemes and fractionated oral apparatuses made possible the assignment of polypeptides to structures within the oral apparatus. Approximately 24 polypeptides, including alpha and beta tubulins, are probable components of the basal body-basal plate complex. At least 5 of the oral apparatus polypeptides, including alpha and beta tubulin, are components of the oral apparatus ciliary axonemes. Approximately 138 polypeptides are components of the oral apparatus framework.

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