The major albumin proteins from pea (<i>Pisum sativum</i> L). Purification and some properties

Croy, R. R. D.; Hoque, Mohammed Shamsul; Gatehouse, John A.; Boulter, D.

doi:10.1042/bj2180795

Cited by 88 publications

(59 citation statements)

References 34 publications

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“…4 In mature PA2 albumin, subunits PA2a and PA2b are thought to associate non-covalently and form homodimers of M r 53 000 and 48 000. 5 All these proteins have been studied in some detail, including the determination of amino acid sequence, cDNA and gene characterisation. 2,3,6 Whereas the functional properties of albumin from rapeseed 7,8 and sun¯ower 9 have been characterised, those of pea albumin are not yet reported.…”

Section: Introductionmentioning

confidence: 99%

Foaming and emulsifying properties of pea albumin fractions and partial characterisation of surface-active components

Lu¹,

Quillien²,

Popineau³

2000

J. Sci. Food Agric.

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Section: Introductionmentioning

confidence: 99%

Foaming and emulsifying properties of pea albumin fractions and partial characterisation of surface-active components

Lu¹,

Quillien²,

Popineau³

2000

J. Sci. Food Agric.

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“…LS-24 shows significant sequence identity with albumin 2 from garden pea (Croy et al, 1984;Harris and Croy, 1985;Gruen et al, 1987;Higgins et al, 1987;Jenne, 1991) and chickpea (Cicer arietinum; Kolberg et al, 1983;Vioque et al, 1998). They are associated with metabolic processes being cytoplasmic in localization (Harris and Croy, 1985), in contrast to the other seed storage proteins that are found in membrane-bound vesicles (Larkins and Hurkman, 1978;Okita and Rogers, 1996).…”

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confidence: 99%

Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

et al. 2010

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A regulatory protein from grass pea (Lathyrus sativus), LS-24, a close homolog of albumin 2 from garden pea (Pisum sativum) that is associated with polyamine biosynthesis, was characterized and the structure of a hemopexin-type fold among plant proteins illustrated. Crystal structure of LS-24 determined at 2.2 Å resolution by multiple isomorphous replacement phasing showed four-bladed b-propeller structure having a pseudo 4-fold molecular symmetry along a metal ion-binding central channel. The structure represents typical mammalian hemopexin fold with discernible features correlated with the possible functional variations. The protein was found to exist in the dimeric state. While LS-24 dimer binds to spermine in the crystal structure as well as in solution, binding of heme in solution resulted in the dissociation of the dimer into monomers with concomitant release of bound spermine. Interactions of heme and spermine with LS-24 bear physiological implications. While binding of spermine to LS-24 can be linked with polyamine biosynthesis that of heme correlates with oxidative stress. Mutually exclusive binding of heme and spermine in different oligomeric states suggest a role for LS-24 in sensing oxidative stress through a ligand-regulated monomer-dimer transition switch.

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“…It could also be resulting from post translational proteolysis and subsequent modifications (e.g. deamination of glutamine or asparagine) [30].…”

Section: Discussionmentioning

confidence: 99%

Partial characterization of polypeptide components of sunflower (Helianthus annuus L.) seed albumin fraction

Decherf-Hamey

Mimouni

Raymond

et al. 1990

Nahrung

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The albumin fraction of sunflower seed (Helimthus unnuus, cv. Mirasol) is a family of water soluble basic polypeptides which constitutes about 20% of the seed proteins. This fraction, isolated by selective isoelectric precipitation of globulins, has been studied in detail by sodium dodecyl sulphate gel electrophoresis, non equilibrium pH gradient electrophoresis and combination of these techniques using non reducing and reducing conditions. The molecular mass of the main polypeptides was markedly different between unreduced (12,000 to 16,500 g . mol-') and reduced form (l0,OOO to 18,000 g . mol-I). As shown by NEPHGE mobility of these polypeptides was also altered by reduction. From these results and other observations is concluded that the stability of the globular structure of some polypeptides is dependent on the presence of intact disulphide crosslink(s). By multidimensional gel electrophoresis it was shown that the polypeptide components of each molecular mass classes displayed a high heterogeneity in net charge. Thus ion exchange chromatography procedures allowed only partial separation of different polypeptidic groups. Their amino acid composition shows that some of these fractions are, on the basis of their lysine and sulphur containing amino acids, of nutritional interest. IntroductionAnalogous with other seeds, interest in sunflower seed protein has been concentrated on the salt soluble 11 S globulin (helianthinin) which constitutes the bulk of the seed proteins [l -41. The water soluble seed proteins, the albumin fraction, often referred to as 2s proteins, which constitutes about 20 % of the seed proteins is characterized by relative high contents of sulphur-containing amino acid and lysine [q as in legumes [q and oil seeds

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The major albumin proteins from pea (Pisum sativum L). Purification and some properties

Cited by 88 publications

References 34 publications

Foaming and emulsifying properties of pea albumin fractions and partial characterisation of surface-active components

Foaming and emulsifying properties of pea albumin fractions and partial characterisation of surface-active components

Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

Partial characterization of polypeptide components of sunflower (Helianthus annuus L.) seed albumin fraction

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