Vegetative storage proteins in the tropical tree Swietenia macrophylla: seasonal fluctuation in relation to a fundamental role in the regulation of tree growth

2003 ◽  
Vol 81 (5) ◽  
pp. 492-500 ◽  
Author(s):  
Wei-Min Tian ◽  
Ji-Lin Wu ◽  
Bing-Zhong Hao ◽  
Zheng-Hai Hu
Keyword(s):  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seasonal Fluctuation ◽  
Cambial Activity ◽  
Growth Cycle ◽  
Annual Growth ◽  
Swietenia Macrophylla ◽  
Vegetative Storage Proteins ◽  
Small Roots

The protein-storing cells in Swietenia macrophylla King were investigated. They were found to be of the Populus type, i.e., ordinary parenchyma cells containing both vacuole protein inclusion and starch grains. Vegetative storage proteins with molecular masses of 18 and 21 kDa were separated by SDS–PAGE (sodium dodecyl sulfate – polyacrylamide gel electrophoresis). Immunoblotting with the 21-kDa protein antiserum showed that the 18- and 21-kDa proteins shared common epitopes. The 21-kDa protein and presumably the 18-kDa protein were demonstrated by immunogold labeling to be the main components of the vacuole protein inclusion of the protein-storing cells. At the late stage of an annual growth cycle, vegetative storage proteins were found in the branchlets, trunk, large roots, and small roots. They were stored in large amounts in the secondary phloem of these organs and also in the secondary xylem of the terminal branchlets and small roots. In a new growth cycle, the consumption of the previously accumulated vegetative storage proteins began in the terminal branchlets of the last growth cycle. The vegetative storage proteins in the branchlets were exhausted completely when the new shoot leaves matured, while the storage proteins in the trunk and large roots had no detectable changes in abundance. On the other hand, the tree started to accumulate the two proteins in the stem of the new shoots as early as 1 week after the new shoot leaves matured. These results suggested that the previously accumulated vegetative storage proteins were used for new shoot growth and cambial activity in preference to the newly assimilated nitrogen and that vegetative storage proteins existed in considerable amounts in the stems throughout an annual growth cycle. This seasonal fluctuating pattern of vegetative storage proteins in the whole tree may be an important mechanism by which the tree regulates its growth.Key words: vegetative storage proteins, nitrogen metabolism, Populus-type of protein-storing cells, tropical hardwoods, Swietenia macrophylla King.

Revealing genetic diversity in land races and wild accessions of mungbean [Vigna radiata (L.) Wilczek] using SDS-PAGE of seed storage proteins

2015 ◽  
Author(s):  
Ananya Panda ◽  
Swapan K. Tripathy
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Land Races ◽  
Sds Page ◽  
Wild Accessions ◽  
Total Seed

Total seed storage protein profiles of 74 mungbean land races, three wild accessions and a popular variety ‘Jyoti’ of Odisha were analysed by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). 32 genotypes could be clearly identified based on genotype-specific seed protein fingerprints while rest of the test genotypes were categorized into eight protein types. Genotypes included in each protein type had 100% homology and some of these could be duplicates. In this pursuit, a few specific polypeptide markers have been detected for identification of the land races/ genotypes. Dendrogram based on electrophoretic data clustered the genotypes into seven groups at 70% phenon level. Paralakhemundi local, Samarjhola local and Phulbani local-D; and three wild accessions (TCR 20, TCR 213 and TCR 243) were comparatively divergent from other genotypes. Besides, Jyoti, Kalahandi local 2A, Sikri local, kodala local A and TCR 20 were identified to be protein rich with high seed yield. TCR 20 being morphologically similar to mungbean, moderately high protein content and high yielding as well as resistant to drought and bruchids; it may serve as a valuable source genotype in recombination breeding

The high-molecular-weight glutenin subunit composition of Japanese hexaploid wheat landraces

2000 ◽  
Vol 51 (6) ◽  
pp. 673 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Storage Proteins ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Landraces

The endosperm storage proteins of 174 Japanese wheat (Triticum aestivum) landraces were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine their high-molecular-weight (HMW) glutenin subunit composition. These are alleles for complex gene loci, Glu-A1, Glu-B1, and Glu-D1, that are present in Japanese hexaploid wheat landraces. These were identified by comparison with the subunit mobility previously found in hexaploid wheat. Twenty-four different, major glutenin HMW subunits were identified. Each landrace contained 3–5 subunits, and 17 different glutenin subunit patterns were observed for 13 alleles in Japanese landraces. Japanese landraces showed specific allelic variation in glutenin HMW subunits, different from those in non-Japanese hexaploid wheats.

scholarly journals Cold Acclimation and Alterations in Dehydrin-like and Bark Storage Proteins in the Leaves of Sibling Deciduous and Evergreen Peach

1996 ◽  
Vol 121 (5) ◽  
pp. 915-919 ◽  
Author(s):  
Rajeev Arora ◽  
Michael Wisniewski ◽  
Lisa J. Rowland
Keyword(s):  
Cold Acclimation ◽  
Gel Electrophoresis ◽  
Prunus Persica ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Subzero Temperature ◽  
Protein Gel ◽  
Bark Storage Proteins ◽  
High Level

Seasonal changes in cold tolerance and proteins were studied in the leaves of sibling deciduous and evergreen peach [Prunus persica (L.) Batsch]. Freezing tolerance [defined as the subzero temperature at which 50% injury occurred (LT50)] was assessed using electrolyte leakage. Proteins were separated by sodium dodecyl sulfate polyacrylamide-gel electrophoresis. Electroblots were probed with anti-dehydrin and anti-19-kD peach bark storage protein (BSP) antibodies. Leaf LT50 decreased successively from -5.8 °C on 18 Aug. to -10.3 °C in the evergreen genotype and from -7.0 °C to -15.0 °C in the deciduous genotype by 14 Oct. Protein profiles and immunoblots indicated the accumulation of a 60- and 30-kD protein during cold acclimation in the leaves of deciduous trees; however, levels of these proteins did not change significantly in the evergreen trees. Immunoblots indicate that the 60-kD protein is a dehydrin-like protein. Gel-electrophoresis and immunoblots also indicated that the 19-kD BSP progressively disappeared from summer through fall in leaves of deciduous peach but accumulated to a high level in bark tissues. A similar inverse relationship was not evident in evergreen peach.

An approach for isolating high-molecular-weight glutenin subunit genes using monoclonal antibodies

Genome ◽  
2006 ◽  
Vol 49 (2) ◽  
pp. 181-189 ◽  
Author(s):  
H Q Wang ◽  
X Y Zhang
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Triticum Aestivum ◽  
Amino Acid ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunits ◽  
Sds Page

High-molecular-weight glutenin subunits (HMW-GSs) play an important role in the breadmaking quality of wheat flour. In China, cultivars such as Triticum aestivum 'Xiaoyan No. 6' carrying the 1Bx14 and 1By15 glutenin subunits usually have attributes that result in high-quality bread and noodles. HMW-GS 1Bx14 and 1By15 were isolated by preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and used as an antigen to immunize BALB/c mice. A resulting monoclonal antibody belonging to the IgG1 subclass was shown to bind to all HMW-GSs of Triticum aestivum cultivars, but did not bind to other storage proteins of wheat seeds in a Western blot analysis. After screening a complementary DNA expression library from immature seeds of 'Xiaoyan No. 6' using the monoclonal antibody, the HMW-GS 1By15 gene was isolated and fully sequenced. The deduced amino acid sequence showed an extra stretch of 15 amino acid repeats consisting of a hexapeptide and a nonapeptide in the repetitive domain of this y-type HMW subunit. Bacterial expression of a modified 1By15 gene, in which the coding sequence for the signal peptide was removed and a BamHI site eliminated, gave rise to a protein with mobility identical to that of HMW-GSs extracted from seeds of 'Xiaoyan No. 6' via SDS-PAGE. This approach for isolating genes using specific monoclonal antibody against HMW-GS genes is a good alternative to the extensively used polymerase chain reaction (PCR) technology based on sequence homology of HMW-GSs in wheat and its relatives.Key words: wheat, HMW-GS, monoclonal antibody, immunoscreen.

Diversity of seed storage proteins in common wheat (Triticum aestivum L.)

2011 ◽  
Vol 9 (2) ◽  
pp. 256-259
Author(s):  
Zuzana Šramková ◽  
Edita Gregová ◽  
Svetlana Šliková ◽  
Ernest Šturdík
Keyword(s):  
Triticum Aestivum ◽  
Common Wheat ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel

The objective of our study was to determine the composition of high-molecular weight-glutenin subunits (HMW-GS) in 120 cultivars of common wheat (Triticum aestivum L.). Fourteen alleles and 34 allelic compositions were detected using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The most frequent HMW-GS alleles at the Glu-A1, Glu-B1 and Glu-D1 loci were null (57.1%), 7+9 (43.3%) and 5+10 (61.9%), respectively. However, low-frequency HMW-GS alleles were also observed, such as 13+16, 20, 21, 7 and 18, encoded by the Glu-B1 locus, and 4+12, encoded by the Glu-D1 locus. The wheat–rye 1BL.1RS translocation was identified in 25 cultivars, using acid polyacrylamide gel electrophoresis. The Glu-score varied greatly, and some lines reached the maximum value of 10.

scholarly journals Fluctuation of Vegetative Storage Proteins in the Seedlings of Swietenia macrophylla, Analogous to the Seasonal Changes of Those in the Shoot of the Adult Tree

2007 ◽  
Vol 49 (3) ◽  
pp. 362-367
Author(s):  
Ya-Qin Han ◽  
Xing-Fu Yan ◽  
Hua Zhang ◽  
Zheng-Hai Hu ◽  
Bing-Zhong Hao ◽  
...  
Keyword(s):  
Seasonal Changes ◽  
Storage Proteins ◽  
Swietenia Macrophylla ◽  
Vegetative Storage Proteins ◽  
Adult Tree

scholarly journals Use of Seed Protein Profiles to Characterize Peanut Cultivars1

1994 ◽  
Vol 21 (2) ◽  
pp. 152-159 ◽  
Author(s):  
C. M. Bianchi-Hall ◽  
R. D. Keys ◽  
H. T. Stalker
Keyword(s):  
Seed Protein ◽  
Cultivar Identification ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Genetic Material ◽  
Seed Storage Proteins ◽  
Molecular Techniques ◽  
Protein Profiles ◽  
Sds Page

Abstract In the last 10 to 15 yr, the development of biotechnology and molecular techniques has allowed great advancements toward the identification of cultivars among plant species. In legumes, the success of cultivar identification depends on the species under investigation, the type and variability of genetic material found in cultivars, and the technology used for investigations. In this study, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to assess diversity of peanut (Arachis hypogaea L.) seed protein profiles. The objectives of this investigation were a) to assess diversity of protein profiles in peanuts for cultivar identification using SDS-PAGE and b) to determine the extent of variability of seed storage proteins (SSP) among samples of cultivars originating from different locations. The first study included 34 cultivars grown at Lewiston, NC and the second one included nine cultivars grown at six locations. The results of both studies indicated that it is possible to differentiate between subspecies but not to associate a particular profile with only one specific cultivar. Within subspecies, cultivars clustered in more than one group and most cultivars that grouped together were genetically related.

Recombination of alleles conferring specific resistance to powdery mildew at the Mla locus in barley

Genome ◽  
1994 ◽  
Vol 37 (3) ◽  
pp. 460-468 ◽  
Author(s):  
Mamatha Mahadevappa ◽  
Richard A. DeScenzo ◽  
Roger P. Wise
Keyword(s):  
Powdery Mildew ◽  
Storage Proteins ◽  
Specific Resistance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Genetic Distances ◽  
Hordeum Vulgare L ◽  
Powdery Mildew Fungus ◽  
Barley Powdery Mildew ◽  
Mla Locus

In barley (Hordeum vulgare L.), the Mla locus conditions reaction to the powdery mildew fungus Erysiphe graminis f.sp. hordei. Enrichment for genetic recombinants in the Mla region is possible by screening for recombination events between the flanking endosperm storage proteins hordeins C and B. Reciprocal crosses were made between the Franger (C.I. 16151) and Rupee (C.I. 16155) lines carrying the (Mla6 + Mla14) and Mla13 alleles, respectively. Recombinants were identified from F2 segregants by analyzing the extracted hordein polypeptides by sodium dodecyl sulphate – polyacrylamide gel electrophoresis. Two hundred and seventy-six recombinant gametes were identified from the 1800 seeds that were screened. Recombination of Mla alleles was analyzed by inoculating F4 recombinant lines with three isolates of E. graminis (A27, 5874, and CR3), which recognize specific Mla alleles. The linkage order established is Hor1–Mla6–Mla13–Mla14–Hor2. The genetic distances between Hor1–Mla6, Mla6–Mla13, and Mla13–Hor2, obtained using Mapmaker 3.0b F3 intercross analysis, are 3.9, 0.2, and 5.2 cM, respectively.Key words: recombinant, barley, powdery mildew, Mla, hordein.

DISTRIBUTION AND ULTRASTRUCTURE OF VEGETATIVE STORAGE PROTEINS IN LEGUMINOSAE

IAWA Journal ◽  
2004 ◽  
Vol 25 (4) ◽  
pp. 459-499 ◽  
Author(s):  
Wei-Min Tian ◽  
Zheng-Hai Hu
Keyword(s):  
Storage Proteins ◽  
Light And Electron Microscopy ◽  
Protein Body ◽  
Seasonal Fluctuation ◽  
Vegetative Storage Protein ◽  
Molecular Weights ◽  
Vegetative Storage Proteins ◽  
Cell Type Specific ◽  
Vacuolar Protein ◽  
Protein Rich

The distribution and ultrastructure of vegetative storage proteins in 44 species and one variety of 31 genera of Leguminosae were investigated by light- and electron microscopy and SDS-PAGE. Leguminosae are as a whole a vegetative storage protein-rich family, abundant with vacuolar protein inclusions in deciduous trees while much less so in evergreen trees. Several prominent proteins with molecular weights ranging from 15 to 45 kDa were isolated and identified to be vegetative storage proteins on the basis of their association with vacuolar protein inclusions and seasonal fluctuation. Vacuolar protein inclusions were present in protein body-like organelles in temperate species while localized in large central vacuoles in tropical ones during leafless periods. The inclusions varied in forms among species or in the same species, but the different forms were present in different cells, suggesting that vegetative storage proteins may be cell-type specific to some extent.

The high-molecular-weight glutenin subunit composition of Australian wheat cultivars

1986 ◽  
Vol 37 (2) ◽  
pp. 125 ◽  
Author(s):  
GJ Lawrence
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Cultivars ◽  
Australian Wheat ◽  
Hmw Glutenin

The seed storage proteins of 106 Australian wheat cultivars were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine the allelic composition of the cultivars at each of the three loci controlling high-molecular-weight (HMW) glutenin subunits. Amongst the cultivars, three alleles were identified at the Glu-A1 locus, eight at the Glu-B1locus and four at the Glu-D1 locus. The results are presented in the form of a key to aid identification of unknown samples. Sixteen of the cultivars were found to consist of two or more biotypes with respect to HMW glutenin subunit composition.

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