Relationship between alcohol-soluble proteins extracted from maize endosperm by different methods

Landry, Jacques; Fey, Dennis A.; Paulis, J.W.

doi:10.1021/jf00120a042

Cited by 21 publications

(21 citation statements)

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“…It also contained more histidine, arginine, proline, and methionine than did a-zein which Paulis (20) attnbuted to the presence ofthe 14 kD component in (#-zein. Alcoholsoluble reduced glutelin, or zein-2, was separated into two subfractions, water-soluble and water-insoluble, by dialysis against water (8,18).The same fraction was also separated into five subfractions by ion-exchange chematography (2). Two of these subfractions, 4 and 5, and a protein isolated by Wilson et al (25), reduced-soluble protein, are now known to be the same as the water-soluble alcohol-soluble reduced glutelin isolated by Paulis and Wall (18).…”

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“…As for ,-zein, it failed to enter polyacrylamide gel without reduction but, after reduction, entered the gel and displayed three predominant size components with mol wts of 24, 22, and 14 kD. It also contained more histidine, arginine, proline, and methionine than did a-zein which Paulis (20) (8,18).The same fraction was also separated into five subfractions by ion-exchange chematography (2). Two of these subfractions, 4 and 5, and a protein isolated by Wilson et al (25), reduced-soluble protein, are now known to be the same as the water-soluble alcohol-soluble reduced glutelin isolated by Paulis and Wall (18).…”

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Separation of Alcohol-Soluble Proteins (Zeins) from Maize into Three Fractions by Differential Solubility

1986

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ABSITRACTThe prolamin of maize (Zea mays L.), zein, was extracted from endosperm meal with 60% (v/v) 2-propanol/1% (v/v) 2-mercaptoethanol either directly or subsequent to extraction with 90% (v/v) 2-propanol. The zein extracted with 90% 2-propaol was essentially made up of 20 to 24 kilodalton polypeptides (cf-zein) while that exltactble with 60% 2-propanol/1% 2-mercaptoethanol containd, in addition to a-zein, 17 to 18 kilodlton methionine-rich polypeptides and a 27 kilodalton prolinerich polypeptide. While zein was separated into three fractions by differential solubility in 90% 2-propanol and 30% 2-propanol/30 millimolar sodium acetate (pH 6) using two different fractionation protocols. (23) from maize endosperm meal. Extractability, solubility, amino acid and electrophoretic analyses showed that a-zein constituted 35% of total zein, and included two prominent bands with mol wt 22 and 24 kD, respectively, and had an amino acid and polypeptide composition similar to that of whole zein (20). As for ,-zein, it failed to enter polyacrylamide gel without reduction but, after reduction, entered the gel and displayed three predominant size components with mol wts of 24, 22, and 14 kD. It also contained more histidine, arginine, proline, and methionine than did a-zein which Paulis (20) attnbuted to the presence ofthe 14 kD component in (#-zein. Alcoholsoluble reduced glutelin, or zein-2, was separated into two subfractions, water-soluble and water-insoluble, by dialysis against water (8,18).The same fraction was also separated into five subfractions by ion-exchange chematography (2). Two of these subfractions, 4 and 5, and a protein isolated by Wilson et al. (25), reduced-soluble protein, are now known to be the same as the water-soluble alcohol-soluble reduced glutelin isolated by Paulis and Wall (18).A simple fractionation scheme to permit separation of zein into fractions of unique polypeptide composition by differential solubility has been a subject of continuous investigation for the author in the last 7 years or so. After countless, mostly unsuccessful, experiments and years of painstaking effort such a procedure has been developed. This procedure, which separates the maize prolamin, zein, into three fractions each with unique polypeptide composition, is described and discussed in this report. MATERUILS AND METHODSPreparation of Cornmeal. Sources of maize seeds used for zein isolation were inbreds K55 and W64A. Endosperm meal was prepared from kernels whose germ and pericarp had been removed after soaking in water for 30 to 60 min. Endosperms were ground first in a mill and then by pestle in a mortar to pass a 150 um sieve. The corn meals so prepared were stored in a freezer with or without prior defatting with hexanes.

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Separation of Alcohol-Soluble Proteins (Zeins) from Maize into Three Fractions by Differential Solubility

1986

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“…When separated by SDS-PAGE, y-zein gives a broad (diffuse) band with an estimated mol wt of 27 kD (6). The analysis of y-zein fraction isolated by differential solubility at low pH indicated the presence of at least two size classes (14).…”

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Primary Structure of a Proline-Rich Zein and Its cDNA

Wang¹,

Esen²

1986

Plant Physiol.

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Eighty-five cDNA clones for 'y-zein (proline-rich zein) from a cDNA expression library were isolated using specific antibody and cDNA probes. Nucleotide sequences of seven independent clones were determined and found to be identical in regions where they overlapped. The primary structure of the mature protein, determined from the sequence of one near full-length clone, consists of 204 amino acids. It has a molecular weight of 21,824 daltons, about 5 kilodaltons less than that estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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“…It is interesting to compare the electrophoretic data of Figure 1 with those reported by Landry et al (1983), who isolated an extract using 55% 2-propanol plus 1.2% 2ME from endosperm meal previously treated by saline and then alcoholic solutions, in the absence of a reducing agent ( Figure 2). This extract, referred to as G 1 -glutelins by Landry and Moureaux (1970), contained all of the bands evident in the patterns of the three extracts depicted in Figure 1, excluding the 12 kDa band.…”

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confidence: 79%

“…Furthermore, G 2 -glutelins were partially coextracted with G 1 -glutelins if salt was not removed from meal exhaustively (Landry et al, 1983) (this has been rediscovered in 1990 by Wallace et al) and could be isolated from the latter as a water-soluble fraction. G 2 -glutelins can also be solubilized after salt extraction and before alcohol extraction with 0.5 M NaCl plus 0.6% (v/v) 2-mercaptoethanol (2ME) using solvent sequence B (Landry and Moureaux, 1970) and were used by Wilson et al (1981) to isolate reduced soluble proteins.…”

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confidence: 97%

Isolation and Quantitation of Zeins in Waxy and Amylose-Extender and Wild Flint and Dent Maize Endosperm Using a New Solvent Sequence for Protein Extraction

Landry

Delhaye

Philippeau

et al. 2000

J. Agric. Food Chem.

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Protein distribution in endosperm of maize grains differing by their texture, flint or dent, and by their genotype, wild or waxy or amylose-extender, was examined by the successive use of 0.5 M NaCl, 0.5 M NaCl plus 0.6% 2-mercaptoethanol (2ME) at neutral and then alkaline pH, and 55% 2-propanol plus 0.6% 2ME as extractants. Proteins extracted in the presence of 2ME were characterized by their size polymorphism and amino acid composition. Proteins isolated with NaCl plus 2ME at neutral pH corresponded with a mixture of gamma-zein (27 kDa) and glutelin-like proteins. Proteins isolated with NaCl plus 2ME at pH 10 were a mixture of gamma-zeins (27 and 16 kDa) and beta-zeins (14 kDa). Alcohol-soluble proteins consisted of alpha-, beta-, and delta-zeins, alpha subunits being predominant. Zein quantitation was improved by weighing the nitrogen percentage of extracts by their zein content, as estimated from the data on amino acid composition. The data reported by Wolf et al. (Cereal Chem. 1975, 52, 765) were integrated to the results of this work to suggest the occurrence of an inverse correlation between amylose in starch and zeins in proteins.

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Relationship between alcohol-soluble proteins extracted from maize endosperm by different methods

Cited by 21 publications

References 13 publications

Separation of Alcohol-Soluble Proteins (Zeins) from Maize into Three Fractions by Differential Solubility

Separation of Alcohol-Soluble Proteins (Zeins) from Maize into Three Fractions by Differential Solubility

Primary Structure of a Proline-Rich Zein and Its cDNA

Isolation and Quantitation of Zeins in Waxy and Amylose-Extender and Wild Flint and Dent Maize Endosperm Using a New Solvent Sequence for Protein Extraction

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