Grain proteins as markers of genetic traits in wheat

2001 ◽  
Vol 52 (12) ◽  
pp. 1161 ◽  
Author(s):  
G. B. Cornish ◽  
D. J. Skylas ◽  
S. Siriamornpun ◽  
F. Békés ◽  
O. R. Larroque ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Reversed Phase ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Phenotypic Data ◽  
Genetic Traits ◽  
Wheat Lines ◽  
New Protein

Different protein fractionation techniques were used to define differences between a set of 8 wheat lines used in genetic mapping studies in Australia. A proteomics approach was used to establish the feasibility of identifying new protein polymorphisms for mapping purposes. Detailed analysis confirmed differences in the glutenin subunits, gliadin proteins, and 10–20 other proteins, between the mapping population parents, Cranbrook, Halberd, CD87, and Katepwa. Differences were particularly evident in the low molecular weight classes of protein. Alternative technologies were used to determine the differences in various protein classes in order to screen doubled haploid lines derived from crosses between the wheat lines. Polyacrylamide gel electrophoresis analysis allowed the mapping of loci encoding high molecular weight (HMW) and low molecular weight (LMW) glutenin subunit proteins. Reversed phase high performance liquid chromatography also allowed several loci encoding LMW glutenin subunit proteins to be mapped, as well as a new protein on chromosome 6A. Capillary electrophoresis provided a high-resolution system that was used to map several gliadin-type proteins. The studies showed that proteins provide useful genetic markers and the data are discussed from the point of view of the advantages that protein-based markers offer in providing both genotypic and phenotypic data.

scholarly journals Proteomic Determination of Low-Molecular-Weight Glutenin Subunit Composition in Aroona Near-Isogenic Lines and Standard Wheat Cultivars

2021 ◽  
Vol 22 (14) ◽  
pp. 7709
Author(s):  
Kyoungwon Cho ◽  
You-Ran Jang ◽  
Sun-Hyung Lim ◽  
Susan B. Altenbach ◽  
Yong Q. Gu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Allelic Variation ◽  
Reversed Phase ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Near Isogenic Lines ◽  
Wheat Cultivars ◽  
Reliable Determination ◽  
Isogenic Lines

The low-molecular weight glutenin subunit (LMW-GS) composition of wheat (Triticum aestivum) flour has important effects on end-use quality. However, assessing the contributions of each LMW-GS to flour quality remains challenging because of the complex LMW-GS composition and allelic variation among wheat cultivars. Therefore, accurate and reliable determination of LMW-GS alleles in germplasm remains an important challenge for wheat breeding. In this study, we used an optimized reversed-phase HPLC method and proteomics approach comprising 2-D gels coupled with liquid chromatography–tandem mass spectrometry (MS/MS) to discriminate individual LMW-GSs corresponding to alleles encoded by the Glu-A3, Glu-B3, and Glu-D3 loci in the ‘Aroona’ cultivar and 12 ‘Aroona’ near-isogenic lines (ARILs), which contain unique LMW-GS alleles in the same genetic background. The LMW-GS separation patterns for ‘Aroona’ and ARILs on chromatograms and 2-D gels were consistent with those from a set of 10 standard wheat cultivars for Glu-3. Furthermore, 12 previously uncharacterized spots in ‘Aroona’ and ARILs were excised from 2-D gels, digested with chymotrypsin, and subjected to MS/MS. We identified their gene haplotypes and created a 2-D gel map of LMW-GS alleles in the germplasm for breeding and screening for desirable LMW-GS alleles for wheat quality improvement.

Efficient purification of low molecular weight nitrogen polar compounds from the skin of Bufo bufo gargarizans Cantor by reversed-phase high performance liquid chromatography with a polar-copolymerized C18 stationary phase

2014 ◽  
Vol 6 (14) ◽  
pp. 5183-5190 ◽  
Author(s):  
Xiaolong Li ◽  
Runqi Huang ◽  
Yanfang Liu ◽  
Hongli Jin ◽  
Huihui Wan ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Stationary Phase ◽  
High Performance ◽  
Polar Compounds ◽  
Bufo Bufo ◽  
Reversed Phase ◽  
Low Molecular Weight ◽  
Toad Skin ◽  
Bufo Gargarizans ◽  
Novel Method

A novel method based on the polar-copolymerized C18 stationary phase was developed to separate polar compounds from toad skin.

A glyco-phosphoprotein in human milk

1987 ◽  
Vol 54 (2) ◽  
pp. 199-205 ◽  
Author(s):  
Norihiro Azuma ◽  
Kunio Yamauchi
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Gel Electrophoresis ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Reversed Phase ◽  
Ultracentrifugal Analysis

SummaryA highly glycosylated phosphoprotein (HGPP) was isolated from a human casein fraction by reversed-phase high-performance liquid chromatography. This component contained carbohydrates to ∼ 38·2% (w/w) and phosphorus to ∼ 1·6% (w/w). The molecular weight of this HGPP as estimated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis ∼ 41000. Ultracentrifugal analysis revealed that the sedimentation coefficient of the HGPP was 2·6S in a 10 mM-imidazole-HCl buffer at pH 7·0 and 27 °C, but this component interacted with human κ-casein and formed a complex with s = 10·4S.

A high-performance oil-free backing pump for electron microscopes

1978 ◽  
Vol 36 (1) ◽  
pp. 110-111
Author(s):  
G.K.W. Balkau ◽  
E. Bez ◽  
J.L. Farrant
Keyword(s):  
Molecular Weight ◽  
Electron Microscope ◽  
Hot Spots ◽  
High Performance ◽  
Carbonaceous Material ◽  
Contamination Rate ◽  
Low Molecular Weight ◽  
Principal Source ◽  
Rotary Pumps ◽  
Electron Microscopes

The earliest account of the contamination of electron microscope specimens by the deposition of carbonaceous material during electron irradiation was published in 1947 by Watson who was then working in Canada. It was soon established that this carbonaceous material is formed from organic vapours, and it is now recognized that the principal source is the oil-sealed rotary pumps which provide the backing vacuum. It has been shown that the organic vapours consist of low molecular weight fragments of oil molecules which have been degraded at hot spots produced by friction between the vanes and the surfaces on which they slide. As satisfactory oil-free pumps are unavailable, it is standard electron microscope practice to reduce the partial pressure of organic vapours in the microscope in the vicinity of the specimen by using liquid-nitrogen cooled anti-contamination devices. Traps of this type are sufficient to reduce the contamination rate to about 0.1 Å per min, which is tolerable for many investigations.

scholarly journals Simultaneous Determination of Human Serum Albumin and Low-Molecular-Weight Thiols after Derivatization with Monobromobimane

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3321
Author(s):  
Katarzyna Kurpet ◽  
Rafał Głowacki ◽  
Grażyna Chwatko
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Simultaneous Determination ◽  
Reversed Phase ◽  
Fluorescence Labeling ◽  
Detector Response ◽  
Low Molecular Weight

Biothiols are extremely powerful antioxidants that protect cells against the effects of oxidative stress. They are also considered relevant disease biomarkers, specifically risk factors for cardiovascular disease. In this paper, a new procedure for the simultaneous determination of human serum albumin and low-molecular-weight thiols in plasma is described. The method is based on the pre-column derivatization of analytes with a thiol-specific fluorescence labeling reagent, monobromobimane, followed by separation and quantification through reversed-phase high-performance liquid chromatography with fluorescence detection (excitation, 378 nm; emission, 492 nm). Prior to the derivatization step, the oxidized thiols are converted to their reduced forms by reductive cleavage with sodium borohydride. Linearity in the detector response for total thiols was observed in the following ranges: 1.76–30.0 mg mL−1 for human serum albumin, 0.29–5.0 nmol mL−1 for α-lipoic acid, 1.16–35 nmol mL−1 for glutathione, 9.83–450.0 nmol mL−1 for cysteine, 0.55–40.0 nmol mL−1 for homocysteine, 0.34–50.0 nmol mL−1 for N-acetyl-L-cysteine, and 1.45–45.0 nmol mL−1 for cysteinylglycine. Recovery values of 85.16–119.48% were recorded for all the analytes. The developed method is sensitive, repeatable, and linear within the expected ranges of total thiols. The devised procedure can be applied to plasma samples to monitor biochemical processes in various pathophysiological states.

scholarly journals Composition of low-molecular-weight glutenin subunits in common wheat (Triticum aestivum L.) and their effects on the rheological properties of dough

2021 ◽  
Vol 16 (1) ◽  
pp. 641-652
Author(s):  
Sławomir Franaszek ◽  
Bolesław Salmanowicz
Keyword(s):  
Molecular Weight ◽  
Rheological Properties ◽  
Common Wheat ◽  
High Performance ◽  
Triticum Aestivum L ◽  
Quality Parameters ◽  
Low Molecular Weight ◽  
Wheat Varieties ◽  
Breeding Lines ◽  
Capillary Zone

Abstract The main purpose of this research was the identification and characterization of low-molecular-weight glutenin subunit (LMW-GS) composition in common wheat and the determination of the effect of these proteins on the rheological properties of dough. The use of capillary zone electrophoresis and reverse-phase high-performance liquid chromatography has made it possible to identify four alleles in the Glu-A3 and Glu-D3 loci and seven alleles in the Glu-B3 locus, encoding LMW-GSs in 70 varieties and breeding lines of wheat tested. To determine the technological quality of dough, analyses were performed at the microscale using a TA.XT Plus Texture Analyzer. Wheat varieties containing the Glu-3 loci scheme (Glu-A3b, Glu-A3f at the Glu-A3 locus; Glu-B3a, Glu-B3b, Glu-B3d, Glu-B3h at the Glu-B3 locus; Glu-D3a, Glu-D3c at the Glu-D3 locus) determined the most beneficial quality parameters.

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