Varietal and environmental differences in the proteins of the groundnut (<i>arachis hypogaea</i>)

Dawson, R. M. C.; McIntosh, Alexander

doi:10.1002/jsfa.2740240513

Cited by 26 publications

(12 citation statements)

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“…In part this may be due to the formation of multimeric complexes or disulfide bond interchange (14,15,23). Variable amounts of low mol wt components have also been noted (3,8), possibly the result of proteolysis. In the work presented here, homogenization of the peanut meal in presence of alkaline urea solution, and the subsequent addition of non-ionic detergent and DTT led to almost complete solubilization of all the proteins.…”

Section: Discussionmentioning

confidence: 99%

“…For example, one-dimensional polyacrylamide gel electrophoresis, although widely employed, resolves only a limited number of polypeptides (4,8,10,11,19). In the peanut, the proteins are very poorly defmed and are contained mainly in two major globulin fractions, arachin and conarachin, which together constitute 97% of the protein of the meal.…”

Section: Introductionmentioning

confidence: 99%

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Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Basha¹

1979

Plant Physiol.

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Seed polypeptides from several cultivars of peanut (Arachis hypogaea L.) have been compared by means of a two-dimensional polyacrylamide gel electrophoresis. Protein was extracted from the defatted peanut meal by homogenizing in 5 millimolar K2CO3-9.5 molar urea. After addition of Nonidet P40 (2%, v/v) The peanut (Arachis hypogaea L.) is an economically important source of vegetable protein, but is relatively low in its content of methionine, lysine and tryptophan (1, 11). There are a few reports suggesting that certain genotypes exist within the species that contain a better balance of nutritionally important amino acids than found in commercial cultivars (1,3,11).Current methods for screening variants for differences in protein composition are generally tedious and often inaccurate. For example, one-dimensional polyacrylamide gel electrophoresis, although widely employed, resolves only a limited number of polypeptides (4,8,10,11,19). In the peanut, the proteins are very poorly defmed and are contained mainly in two major globulin fractions, arachin and conarachin, which together constitute 97% of the protein of the meal. Each of these globulins consists of several polypeptide species, which are thought to exist together as subunits of large multimeric complexes. In addition, many of the polypeptides appear to have similar molecular weights (2, 20). In this study I have characterized the proteins of peanut meal using a two-dimensional electrophoretic technique which separates the 'This research was supported in part by National Science Foundation Grant PCM 76-81071 to R. M. Roberts. polypeptides according to their isoelectric point in the first dimension and by subunit size in the second. The method has been employed to distinguish different cultivars according to their polypeptide composition. It also allows application of up to 500 ,ug of protein on a single slab gel, thus providing the potential for purifying significant quantities of individual polypeptide components. MATERIALS AND METHODS SEED MATERIALSeeds from the following peanut (A. hypogaea L.) cultivars were provided by A. J. Norden of the University of Florida from their breeding lines: Florunner, Florigiant, Early Bunch, Jenkins Jumbo Runner, Altika, UF 75102, UF 77318, 439-16-10-3, 439-16-10-3-1, 439-16-10-3-2, and 439-16-10-1-1. After removal of skins and embryonic axes, the cotyledons were ground in a mortar with a pestle. The ground material was then defatted with cold ethyl ether by repeated extractions until the peanut meals were essentially fat-free. The defatted meals were stored at -20 C. CHEMICALS SDS (specially pure) was from British Drug House, Poole, UK.; ampholines were purchased from LKB, Uppsala, Sweden; urea was bought from Pierce Chemical Co., Rockford, Ill., Nonidet P-40 was obtained from Particle Data Laboratories, Ehmhurst, Ill. Coomassie brilliant blue R-250 and N,N'diallyltartardiamide (DATD) were products of Bio-Rad Laboratories, Richmond, Calif. Protein standards and agarose were from Sigma Chemical Co. Reagents f...

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Basha¹

1979

Plant Physiol.

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“…The observed difference may be due to the difference in the variety of rapeseeds under study as such differences are known in the literature for certain plant proteins, e.g. peanut (29).…”

Section: Figurementioning

confidence: 98%

Reconstitution of rapeseed high molecular weight protein from isolated subunits

Bhushan

Mahesh

Mallikharjun

1990

International Journal of Peptide and Protein Research

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The high molecular weight protein was isolated from rapeseed and characterised. Six subunits were isolated in SDS (0.01%) solution on polyacrylamide gel electrophoresis and by gel filtration on Sephadex G‐100. Reassociation by removing SDS by co‐dialysis, against 10mM sodium phosphate buffer (pH 7.9) was done and the yield was about 90%. The reconstituted protein was indistinguishable from the intact protein in all respects. The subunits isolated from the native protein and the reconstituted protein were found to have identical molecular weights and N‐terminal amino acids. No disulphide bonds were observed in the subunit association. Amino acid analysis of the proteins and the six subunits was performed and the number of each amino acid residue calculated.

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“…Unfortunately, little information is available on the influence of the environment on the carotenoid content in potatoes, especially growing seasons and locations. Genotype and environment interactions have been reported to account for alteration in free amino acids, protein, and sugar composition [5][6][7][8][9][10][11][12][13]. In addition, the total glycoalkaloid content of potato tubers was found greatly affected as a result of environmental changes during the growing season [14], even though there are also strong genetic effects [15,16].…”

Section: Introductionmentioning

confidence: 99%

Influence of Environmental Stress toward Carotenogenesis Regulatory Mechanism through In Vitro Model System

Othman¹,

Hassan²,

MohdHatta³

2017

Carotenoids

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Carotenoid biosynthesis is influenced by some aspects and is liable to geometric isomerisation with the existence of oxygen, light, and heat, which affect color degradation and oxidation. The major problems related to carotenoid accumulation inherently originate from pigment instability. This chapter discusses an overview on the influence of stringent control of genetic, developmental, and environmental factors toward carotenoid biogenesis in potato minitubers through the potential model system for rapid initiation, extraction, and analysis of carotenoids. The outcome of this experimental system is a discovery of variables regulating carotenoid accumulation as a result of the environmental change assessment through manipulation of drought stress, light intensity, and nutrient strength on carotenoid accumulation.

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Varietal and environmental differences in the proteins of the groundnut (arachis hypogaea)

Cited by 26 publications

References 12 publications

Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis

Reconstitution of rapeseed high molecular weight protein from isolated subunits

Influence of Environmental Stress toward Carotenogenesis Regulatory Mechanism through In Vitro Model System

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