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 Common structural genes for platelet and plasma fibrinogen

Blood ◽  
1985 ◽  
Vol 65 (1) ◽  
pp. 120-126 ◽  
Author(s):  
B Teige ◽  
G Gogstad ◽  
F Brosstad ◽  
B Olaisen
Keyword(s):  
Plasma Fibrinogen ◽  
Two Dimensional ◽  
Structural Genes ◽  
Gamma Chain ◽  
Two Dimensional Electrophoresis ◽  
Alpha Chain ◽  
Variant Pattern ◽  
Different Sources ◽  
Dimensional Electrophoresis

Abstract Fibrinogen from plasma was compared with fibrinogen from platelets using two-dimensional electrophoresis. The source of platelet fibrinogen was isolated alpha-granules, thrombin- and collagen-released platelet material. The B beta- and gamma-chains from the different sources showed similar two-dimensional patterns, while gamma'-chains were not observed in platelet fibrinogen preparations. Furthermore, the A alpha-chain could hardly be identified in platelet preparations. When individual fibrinogen was studied in persons heterozygous for genetic B beta- and gamma-chain variants, the two-dimensional variant pattern could be demonstrated in plasma fibrinogen as well as in platelet fibrinogen. This observation strongly indicates that the structural genes for plasma and platelet fibrinogen B beta- and gamma-chains are identical.

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.

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

Proteins of human urine. II. Identification by two-dimensional electrophoresis of a new candidate marker for prostatic cancer.

1982 ◽  
Vol 28 (1) ◽  
pp. 160-163 ◽  
Author(s):  
J J Edwards ◽  
N G Anderson ◽  
S L Tollaksen ◽  
A C von Eschenbach ◽  
J Guevara
Keyword(s):  
Sodium Dodecyl ◽  
Prostatic Hyperplasia ◽  
Prostatic Adenocarcinoma ◽  
Relative Molecular Mass ◽  
Urogenital System ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Candidate Marker ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Abstract A protein series common to the urine and prostatic tissue of 16 of 17 patients with prostatic adenocarcinoma has been identified by high-resolution two-dimensional gel electrophoresis. These proteins, designated PCA-1, have a relative molecular mass in sodium dodecyl sulfate of about 40000. Analyses of urines from eight age-matched controls, seven patients with other ty pes of urogenital malignancies, two patients with benign prostatic hyperplasia, and five patients with malignancies not associated with the urogenital system failed to show PCA-1 in the patterns. These preliminary findings suggest that this protein should be systematically investigated as a candidate marker for prostatic adenocarcinoma in man.

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