Journal ArticleDOI
Sunflower Seed Proteins: Characterization and Subunit Composition of the Globulin Fraction
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TLDR
Results suggest that a major reserve protein in sunflower seeds is similar to 'legumin' of plants of the family Leguminosae, as shown by ion-exchange chromatography under dissociating and reducing conditions.Abstract:
Salt soluble proteins from sunflower (Helianthus annuus) seeds were fractionated by isoelectric precipitation and analysed by electrophoresis. Three molecular species were detected by gradient polyacrylamide gel electrophoresis of the globulin fraction. Multi-dimensional gel electrophoresis analysis indicates that all these species contained similar intermediary subunits of60 000,54 000,48 000 and 40000 molecular weight, the two former being predominant. As shown by ion-exchange chromatography under dissociating and reducing conditions, the intermediary subunits are composed of disulphide linked pairs of large 'acidic' and small 'basic' subunits. Heterogeneity in molecular weight of these subunits was shown by electrophoretic studies. These results suggest that a major reserve protein in sunflower seeds is similar to 'legumin' of plants of the family Leguminosae.read more
Citations
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Sunflower proteins: overview of their physicochemical, structural and functional properties
TL;DR: This review provides detailed information about sunflower seed composition and processing, including processes to remove phenolic compounds from meals and the structure and functionality of the two major protein fractions, helianthinin and 2S albumins.
Journal ArticleDOI
Purification and some properties of polyphenoloxidase from sunflower seeds
TL;DR: The polyphenoloxidase from Helianthus annuus was purified by a combination of SP-Sephadex G-50 chromatography, DEAE-cellulose chromatography and Sepha.
Journal ArticleDOI
Subunit composition of the globulin fraction of rapeseed (Brassica napus L.)
TL;DR: The notion that native cruciferin is composed of subunits with large and small polypeptides linked by disulphide bonds and of similar or closely-related polypePTides which are not covalently bonded is supported.
Journal ArticleDOI
Sequence and expression of a gene encoding an albumin storage protein in sunflower
Randy D. Allen,E. A. Cohen,R. A. Vonder Haar,C. A. Adams,D. P. Ma,Craig L. Nessler,Terry L. Thomas +6 more
TL;DR: Comparison of the predicted HaG5 gene product with sequences of other known plant proteins revealed distant but significant homology with the napins of Brassica and other heterogeneous seed proteins in the albumin superfamily.
Journal ArticleDOI
Effect of pH and ionic strength modifications on thermal denaturation of the 11S globulin of sunflower (Helianthus annuus).
TL;DR: Helianthinin, the main storage protein of sunflowers, has low water solubility and does not form a gel when heated; this behavior is different from other 11S globulins and limits its food applications, and changes on helian thinin association-dissociation state induced by modifications in pH and ionic strength were analyzed.
References
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Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
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High resolution two-dimensional electrophoresis of proteins.
TL;DR: This technique provides a method for estimation of the number of proteins made by any biological system and can resolve proteins differing in a single charge and consequently can be used in the analysis of in vivo modifications resulting in a change in charge.
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Legumin and vicilin, storage proteins of legume seeds
TL;DR: The physical, chemical and immunological characteristics of the legumin and vicilin preparations from Pisum sativum are summarised and the distributions of proteins with sedimentation coefficients and/or immunological determinants similar to those of legumin this article.
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Occurrence of low molecular weight and high cysteine containing albumin storage proteins in oilseeds of diverse species
TL;DR: It is proposed that 2S albumins are seed storage proteins with a wide distribution and with chemical properties distinct from those of the globulin storage proteins, which play an additional and unique role of providing sulfur reserve for germination.
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Partial characterization of the acidic and basic polypeptides of glycinin.
TL;DR: The glycinin polypeptide composition is more complex than previous reports indicated, and for the first time characterized the variouspolypeptides of the 11 S storage protein by structural analysis.