isolation and determination of the primary structure of a C-hordein gene from barley (Hordeum vulgare cv.Bomi)
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isolation and determination of the primary structure of a C-hordein gene from barley (Hordeum vulgare cv.Bomi)

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Published by University of Birmingham in Birmingham .
Written in English

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Edition Notes

Thesis (M.Sc.) -University of Birmingham, Department of Plant Biology, 1989.

Statementby Joycelyn M. Entwhistle.
ID Numbers
Open LibraryOL13927900M

Download isolation and determination of the primary structure of a C-hordein gene from barley (Hordeum vulgare cv.Bomi)


Small angle X-ray scattering was used to study the solution conformation of the C hordeins of barley (Hordeum vulgare), a group of proteins whose primary structure consists predominantly of . Abstract. The low protein barley (Hordeum vulgare L.) cultivar `Karl' is deficient in hordeins, the major storage protein fraction, but has normal levels of other endosperm protein compared hordein gene expression in Karl with that in `Traill,' a related cultivar that contains normal amounts of by: 7.   The cysteine endoproteases (EP)-A and EP-B were purified from green barley (Hordeum vulgare L.) malt, and their identity was confirmed by N-terminal amino acid sequencing. EP-B cleavage sites in recombinant type-C hordein were determined by N-terminal amino acid sequencing of the cleavage products, and were used to design internally quenched, Cited by: Rothamsted RepositoryCited by:

The grain proteins of barley are deficient in lysine and threonine due to their low concentrations in the major storage protein class, the hordeins, especially in the C-hordein subgroup.   Hordeins, the natural substrates of barley (Hordeum vulgare) cysteine endoproteases (EPs), were isolated as protein bodies and degraded by purified EP-B from green barley malt. Cleavage specificity was determined by synthesizing internally quenched, fluorogenic tetrapeptide substrates of the general formula 2-aminobenzoyl-P2-P1-P1′-P2′ 1-tyrosine(NO2) Cited by:   INTRODUCTION. Barley (Hordeum vulgare L.) is widely used as food and feed, but its most economically important use is for malting and barley characters are involved in malt quality, of which protein content is the most important, as it has been observed to be related to malt qualities, such as extract and diastatic power (Weston et al., ; Eagles et Cited by: The N motif is inverted in S-poor genes from barley (C hordein) and rye (ω-secalin) (Shewry et al., ) but not in the prolamin box of the ω-gliadin gene. Functional analyses of a wheat prolamin promoter were first carried out by introducing LMW subunit gene promoter–chloramphenicol acetyltransferase (CAT) reporter gene constructs into.

Barley (Hordeum vulgare L.) is a globally important grain crop. The composition and structure of barley grain is under genotypic and environmental control during grain development, when storage compounds (mainly starch and protein), are accumulated. Grain structure plays a significant role in malting and feed- and food-processing quality of barley. The development, structure and composition of the barley grain. in: Ullrich, S. E. (ed.) Barley: production, improvement and uses Wiley-Blackwell Chichester, Sussex. pp. Genome sequence of the pea aphid Acyrthosiphon pisumCited by: Introduction. Barley (Hordeum vulgare) has been grown as a cereal crop for thousands of years originating from the area of the Middle East known as the Fertile Crescent (Badr et al., ).It is a temperate dry land crop with a number of uses including as a food, either as a whole grain (e.g., in porridge) or as barley flour for bread making (e.g., in flatbreads), as animal feed Cited by: 1. Hordein polypeptide patterns in relation to malting quality in Brazilian barley varieties (). Cinara Echart-Almeida and Suzana Cavalli-Molina (). Abstract – Since there is evidence that malting quality is related to the storage protein (hordein) fraction, in the present work the hordein polypeptide patterns from 13 barley (Hordeum vulgare L.) varieties of different malting quality .