Genetic variation in wheat endosperm proteins: an analysis by two-dimensional electrophoresis using intervarietal chromosomal substitution lines

1981 ◽  
Vol 59 (6) ◽  
pp. 361-371 ◽  
Author(s):  
J. W. S. Brown ◽  
C. N. Law ◽  
A. J. Worland ◽  
R. B. Flavell
Keyword(s):  
Genetic Variation ◽  
Two Dimensional ◽  
Substitution Lines ◽  
Wheat Endosperm ◽  
Endosperm Proteins ◽  
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 GENETIC VARIATION IN PROTEINS: COMPARISON OF ONE-DIMENSIONAL AND TWO-DIMENSIONAL GEL ELECTROPHORESIS

Genetics ◽  
1983 ◽  
Vol 104 (2) ◽  
pp. 381-390
Author(s):  
Tracy McLellan ◽  
Giovanna Ferro-Luzzi Ames ◽  
Kishiko Nikaido
Keyword(s):  
Genetic Variation ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
One Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Related Proteins ◽  
Dimensional Electrophoresis ◽  
Denaturation Of Proteins ◽  
New Mutations ◽  
Limited Sensitivity

ABSTRACT Two proteins with known characteristics on one-dimensional gels were studied by two-dimensional electrophoresis to compare the sensitivities of the two methods in detecting genetic variation. Two-dimensional electrophoresis was found to be less sensitive than several types of one-dimensional gels in distinguishing variants of both proteins. Denaturation of proteins in urea in the two-dimensional method makes it possible to distinguish closely related proteins that differ from each other by units of charge. Many more types of variation in protein sequences can be distinguished on one-dimensional gels in the absence of denaturants. The estimates of heterozygosity based on two-dimensional gels are lower than those based on other methods, at least in part, because of the limited types of sequence differences that can be detected on two-dimensional gels. The application of two-dimensional electrophoresis to the measurement of genetic variation and to the detection of new mutations should be made carefully, in view of the limited sensitivity of the method in finding differences in sequence.

Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins

1986 ◽  
Vol 7 (1) ◽  
pp. 52-54 ◽  
Author(s):  
Catherine Damerval ◽  
Dominique De Vienne ◽  
Michel Zivy ◽  
Hervé Thiellement
Keyword(s):  
Genetic Variation ◽  
Wheat Seedling ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub
Keyword(s):  
Sialic Acid ◽  
Polypeptide Chain ◽  
Two Dimensional ◽  
Charge Heterogeneity ◽  
Human Fibrinogen ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Polypeptide Chains ◽  
Dimensional Electrophoresis ◽  
Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

Improvement of Two-dimensional Electrophoresis of Rice (Oryza sativaL.) Proteomics

2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN
Keyword(s):  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis
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