Purification, properties and amino acid sequence of a low-<i>M</i>r abundant seed protein from pea (<i>Pisum sativum L.</i>)

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

doi:10.1042/bj2250239

Cited by 36 publications

(14 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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. In this paper, foaming and emulsifying properties of pea albumin were studied and surfaceactive components were partially characterised.…”

Section: Introductionmentioning

confidence: 96%

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

Lu¹,

Quillien²,

Popineau³

2000

J. Sci. Food Agric.

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 96%

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

Lu¹,

Quillien²,

Popineau³

2000

J. Sci. Food Agric.

View full text Add to dashboard Cite

“…as solvent. Peptides were detected by a dilute fluorescamin stain [7] and the cysteine-peptides located by autoradiography. They were eluted with pH-6.5 buffer and lyophilized.…”

Section: Thsl 60mentioning

confidence: 99%

The amino‐acid sequence of the 2S sulphur‐rich proteins from seeds of Brazil nut (Bertholletia excelsa H.B.K.)

Ampè

Damme

Castro

et al. 1986

European Journal of Biochemistry

132

View full text Add to dashboard Cite

Storage proteins of the albumin solubility fraction from seeds of Bertholletia excelsa H.B.K. were separated by reversed-phase high-performance liquid chromatography and their primary structures were determined by gasphase sequencing on intact polypeptides and on the overlapping tryptic and thermolysin peptides. The 2 s storage proteins consist of two subunits linked by disulphide bridges. The large subunit (8.5 kDa) is expressed in at least six different isoforms while the small subunit (3.6 kDa) consists of only one form. These proteins are extremely rich in glutamine, glutamic acid, arginine and the sulphur-containing amino acids cysteine and methionine. One of the variants even contains a sequence of six methionine residues in a row. Comparison with known sequences of 2s proteins of other dicotyledonous plants shows limited but distinct sequence homology. In particular, the positions of the cysteine residues relative to each other appear to be completely conserved, suggesting that tertiary structure constraints imposed by disulphide bridges dominate sequence conservation. It has been proposed that the two subunits of a related protein (the Brassica n a p s storage protein) is cleaved from a precursor polypeptideThe amino acid sequence homology of the Brazil nut protein with the former suggests that a similar protein processing event could occur.Storage proteins are major components of seeds. They are expressed during seed development as long precursors, which undergo co-and post-translational processing before they are deposited, often as protein bodies, in the endosperm, the cotyledons or other tissues of the embryo [l].Several classes of storage proteins are distinguished according to their solubility [2]. The major seed proteins of dicotyledonous plants are the water-soluble albumins, with a sedimentation coefficient of 2s (the 2s proteins), and the globulins which are soluble in high-salt buffers and have a sedimentation coefficient ranging from 7 s to 12s. The plant globulin fraction has been extensively characterized, particularly in nutritionally important legumes and oilseeds. They are generally of high molecular mass and extremely rich in arginine, glutamine and asparagine, amino acids thought to act as nitrogen sources for the developing seedlings [l]. The 2s proteins differ from the globulins in forming a class of lowmolecular-mass proteins which are rich in cysteine. Although some of these proteins have only been recognized recently as storage proteins [3], others, such as the proteinase inhibitors of soybean, have been studied for a long time To date, the complete amino acid sequence of the castor bean (Ricinus communis) and pea (Pisum sativum L.) proteins have been published [6, 71 and the amino acid sequence has been predicted from a cDNA for the rapeseed protein, napin [8]. The castor bean and rapeseed proteins show the same structural organization characterized by two subunits of different size, interlinked by sulphur bridges, while for the pea protein a homodimeric structure has been propo...

show abstract

“…Some of them, like the low-Mr '2S' pea albumin [10], also known as PAl [19], as well as the 2S globulin conglutin b from Lupinus angustifolius [ 11 ], have a limited sequence homology to the above-mentioned group of 2S proteins. Some of them, like the low-Mr '2S' pea albumin [10], also known as PAl [19], as well as the 2S globulin conglutin b from Lupinus angustifolius [ 11 ], have a limited sequence homology to the above-mentioned group of 2S proteins.…”

Section: Discussionmentioning

confidence: 99%

Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: cDNA, gene structure and developmentally regulated formation

et al. 1995

View full text Add to dashboard Cite

cDNA and genomic clones encoding narbonin, a 2S globulin from the seed of narbon bean (Vicia narbonensis L.), were obtained using the polymerase chain reaction (PCR) and sequenced. The full-length cDNA as well as genomic clones contain a single open reading frame (ORF) of 873 bp that encodes a protein with 291 amino acids comprising the mature narbonin polypeptide (M(r) ca. 33 100) and an initiation methionine. The deduced amino acid sequence lacks a transient N-terminal signal peptide. The genomic clones do not contain any intron. No homology was found to nucleic acid and protein sequences so far registered in sequence data libraries. The biosynthesis of narbonin during embryogenesis is developmentally-regulated and its pattern of synthesis closely resembles that of typical seed storage globulins. However, during seed germination narbonin was degraded very slowly, indicating that it may have other function than storage protein. Southern analysis suggests the existence of a small narbonin gene family. Narbonin genes were also found in four different species of the genus Vicia as well as in other legumes such as Canavalia ensiformis and Glycine max. In Escherichia coli a recombinant narbonin was produced which yielded crystals like those prepared from narbonin purified from seeds.

show abstract

Purification, properties and amino acid sequence of a low-Mr abundant seed protein from pea (Pisum sativum L.)

Cited by 36 publications

References 21 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

The amino‐acid sequence of the 2S sulphur‐rich proteins from seeds of Brazil nut (Bertholletia excelsa H.B.K.)

Narbonin, a novel 2S protein from Vicia narbonensis L. seeds: cDNA, gene structure and developmentally regulated formation

Contact Info

Product

Resources

About