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Monday, August 10, 2020 | History

2 edition of Salt-soluble proteins of barley found in the catalog.

Salt-soluble proteins of barley

Robert Djurtoft

Salt-soluble proteins of barley

(hordeum distichum).

by Robert Djurtoft

  • 361 Want to read
  • 11 Currently reading

Published by Dansk Videnskabs Forlag in København .
Written in English


The Physical Object
Pagination239p. :
Number of Pages239
ID Numbers
Open LibraryOL18634568M

In chemistry, a salt is a chemical compound consisting of an ionic assembly of cations and anions. Salts are composed of related numbers of cations (positively charged ions) and anions (negatively charged ions) so that the product is electrically neutral (without a net charge). These component ions can be inorganic, such as chloride (Cl −), or organic, such as acetate (CH. Fig. 2A-D. Developmental pattern of 14C-labeled salt-soluble proteins from barley spikes cultured at different N levels. Proteins were separated by SDS-PAGE and detected by Coomassie Blue (A, D) and fluorography (B, C). A Protein composition at d 15, 20 and 25 after anthesis. The mean endosperm dry weights were , , and

glutelins is valid only for the original barley grain proteins. Because of the changes occurring in high-protein barley flour during processing, the terms water-soluble, salt-soluble, alcohol-soluble, and alkali-soluble protein fractions are used instead of albumins, globulins, prolamins, and glutelins, respectively. Wheat science has undergone countless new developments since the previous edition was published. Wheat: Chemistry and Technology, Fourth Edition ushers in a new era in our knowledge of this mainstay new edition is completely revised, providing the latest information on wheat grain development, structure, and composition including vital peer-reviewed information not readily available.

The hydrophobic salt-soluble proteins from barley were isolated from the chloroform-methanol () extract (hereafter, CM-extract) by gel filtration on Sephadex G followed by chromato graphy on Ultrogel AcA, as described by Aragoncillo et al. (). The protein composition of Brachypodium grain was investigated by separating the proteins on the basis of their solubility combined with a proteomic approach. Salt-soluble proteins as well as salt-insoluble proteins separated by two-dimensional gel electrophoresis revealed .


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Salt-soluble proteins of barley by Robert Djurtoft Download PDF EPUB FB2

Barley protein contents range between 7 and 25%(Ullrich, ) and can be separated into four solubility groups: albumin (water-soluble fraction), globulin (salt-soluble fraction), prolamin or hordein (alcohol-soluble fraction) and glutelins (alkali-soluble fraction) as described by Osborne ().

In the kernel, barley proteins occur in many. Salt-soluble proteins of barley (Hordeum distichum). København, Dansk videnskabs forlag A/S, (OCoLC) Material Type: Thesis/dissertation: Document Type: Book: All Authors / Contributors: Robert Djurtoft.

The lysine content of the individual salt-soluble proteins varied between and %. The existence of three high-lysine protein groups in the salt-soluble protein fraction of barley is suggested.

The significance of these findings in relation to the present work on quality improvement of barley protein is by: Abstract Approximately 10% of the total nitrogen content of barley grain may be extracted from ground barley The salt‐soluble proteins of barley. The non‐protein material is derived mainly from the barley gums and is chiefly precipitated in the fraction precipitated between ‐ saturation with ammonium by: 5.

Abstract. The accumulation of salt-soluble proteins in the endosperm of developing barley (Hordeum vulgare L.) grains was ed spikes of barley were cultured at different levels of nitrogen nutrition and pulse-labeled with [14 C] sucrose at specific times after ns were extracted from isolated endosperms and separated by sodium dodecyl sulfate polyacrylamide gel Cited by:   The salt-soluble proteins in barley grain selected for high-lysine content (Hiproly, CI and the mutants 29 and 86) and of a control (Carlsberg II) with normal lysine content, contain identical major proteins as determined by MW and electrophoretic mobility.

The book is divided into nine chapters, including barley production and consumption, germplasm and utilization, chemical composition, protein and protein components, carbohydrates and sugars. The protein of O.A.C. 21 barley and of the malt produced from it were fractionated by means of various solvents and the fractions were analyzed.

The results of the solubility studies and of the analyses support the use of 5% potassium sulphate for the quantitative separation of the albumin and globulin from the less soluble proteins.

A 4–7 fold increased content of four major salt‐soluble proteins in the barley grain was found to be closely associated with the Hiproly high‐lysine character. The proteins were identified by crossed Immunoelectrophoresis as: “free” β‐amylase, “free” protein Z and two different chymotrypsin inhibitors, with lysine content of 5.

The solubility of proteins is considered as that proportion of nitrogen in a protein product which is in the soluble state under specific conditions. Solubility is the amount of protein in a sample that dissolves into solution.

Proteins recommended as food additives can be partly or completely soluble or completely insoluble in water. Proteases from protein extracts of germinated barley and wheat grains showed the ability to degrade gliadin-derived toxic peptides.

In particular, the C1A protease Triticain-α, formerly thought to participate in seed germination by digesting storage proteins [ 69 ], was shown to possess glutenase activity in vitro [ 70 ].

Abstract. Thirteen new proteins from barley (Hordeum vulgare L.) have been isolated and proteins and seven other previously known components were isolated from a M NaCl extract of endosperm by single-step, reversed-phase, high-performance liquid chromatography, using a Vydac C 4 semi-preparative column.

The purity of the isolated proteins was analyzed by. Barber et al.: Purification of barley salt-soluble proteins TIME (min) Fig. Fractionation by RP-HPLC of salt-soluble barley endosperm proteins.

Top: A solution of salt-soluble proteins ( mg in |il of 10% solvent B) was injected into a Vydac C4 column and.

The in vitro synthesis of nine distinct barley proteins was compared using mRNAs from isolated endosperm and aleurone tissues (developing and mature grain) and from cultured (germinating) aleurone layers treated with abscisic acid (ABA) and GA 3. B and C hordein polypeptides and the salt-soluble proteins β-amylase, protein Z, protein C, the.

Their amino acid composition and solubility properties clearly differ from those of both prolamins and other purified salt-soluble proteins from barley endosperm.

Evidence is presented of their homology with the previously described CM-proteins from wheat. Isolation and characterization of thirteen new salt-soluble proteins from barley by reversed-phase high-performance liquid chromatography.

D Barber Servicio de Endocrinologia, Centro Ramón y Cajal, Carretera de Colmenar Km 9,Madrid. Read "The salt‐soluble proteins of barley. —the detailed composition of saline extracts of barley‐fractionation by precipitation with ammonium sulphate, Journal of the Science of Food and Agriculture" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.

The Glorelated proteins are primarily located in the embryo. Protein expression levels of 7S globulins have been shown to be highest in the embryo and aleurone layers, while almost absent in the endosperm [].To study the expression of Glo-3 proteins, AC Barrie endosperm and embryo salt-soluble protein fractions were compared by two-dimensional (2D) electrophoresis according to pI and M.

In book: Biochemistry of Foods (pp) Mashing is a key step in beer brewing in which starch and proteins are solubilized from malted barley in a hot water extraction and digested to.

A general rule of thumb is a yield of –one pound of barley seed will produce seven pounds of sprouted fodder. Systems for Sprouting Barley. To sprout barley consistently and economically, you need a climate-controlled space, lighting of sufficient brightness (lumens), a soaking vat, a rack and tray system and a watering system.

Proteins account for about 8–15% of the dry weight of the mature barley grain. Albumins and globulins – the water- and salt-soluble proteins, respectively – function as enzymes, metabolic regulators, structural or storage proteins, or inhibitors of particular enzymes.Protein solubility is a thermodynamic parameter defined as a soluble protein concentration that is in equilibrium with a crystalline solid phase influenced by the conditions of pH.Lysine concentration of the grain averaged g/ g protein in four Karl‐type barleys and in seven non‐Karl type barleys, but lysine concentrations on a sample basis (g amino acid/ g barley, dry basis) were andrespectively.

Under conditions of varied N uptake, hordein was the major repository of protein N in Karl barley.