IV. Amino acid composition of the globulins from Lupinus angustifolius and Lupinus luteus

Gerritsen, Th.

doi:10.1016/0006-3002(56)90150-0

Cited by 20 publications

(9 citation statements)

References 8 publications

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“…They also noted the presence of a 2S component but did not report on this further. Amino acid compositions reported by Blagrove and Gillespie (1975) compared favourably with those reported previously (Gerritsen, 1956) while the newly discovered conglutin y, unlike the major 11.6S and 7.8S components, displayed relatively high levels of methionine and lysine. Conglutin y was subsequently verified as being present in storage body extracts, suggesting that this component was indeed a further class of storage protein.…”

Section: Gerritsensupporting

confidence: 77%

“…Conglutin y was not described in the classical studies of Joubert (l955a, 1955bJoubert (l955a, , 1956 or Gerritsen (1956), but emerged in the later study by Blagrove and Gillespie (1975). This component of lupin seed, albeit minor, has greater than the usual levels (see Table I above) of methionine, lysine and cysteine, suggesting a high nutritional value.…”

Section: Conglutin Ymentioning

confidence: 81%

“…After the pioneering studies by Joubert in South Africa during the 1950's (Joubert, 1955a(Joubert, , 1955b(Joubert, , 1955c(Joubert, , 1956(Joubert, , 1957 and others (Naismith, 1955;Petri et al, 1955;Gerritsen, 1956), an interest in the isolation and characterization of lupin seed proteins was rekindled during the 1970's by B1agrove and Gillespie in Australia (Gillespie and Blagrove, 1974;Gillespie, 1975: Gillespie andB1agrove, 1975;Blagrove et ai., 1976: Elleman, 1977: Blagrove and Gillespie, 1978: Gillespic et al, 1978B1agrove et aI., 1980) and by Cerlctti and Duranti in Italy (Duranti and Cerletti. 1979).…”

Section: Historical Perspectivementioning

confidence: 97%

“…Conglutin (5 has been described as a protein of My 25,000 (Gerritsen, 1956), and 44,000 (Duranti et al.1981). The first reported subunit composition for conglutin (5 (from L. albus) suggested two subunits, one of My 21.600 which gave two subunit-polypeptides of M,.…”

Section: Subunit Structurementioning

confidence: 98%

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Lupin Globulins

Lilley¹

1999

Seed Proteins

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Section: Gerritsensupporting

confidence: 77%

Section: Conglutin Ymentioning

confidence: 81%

Section: Historical Perspectivementioning

confidence: 97%

Section: Subunit Structurementioning

confidence: 98%

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Lupin Globulins

Lilley¹

1999

Seed Proteins

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“…Although originally described in 1955 as a sulphur-rich 2S globulin from L. luteus [ 14,21,22], it has only recently been purified and characterized [29,30]. Conglutin b is related to the 2S super-family of storage proteins [25], which is widespread in seeds of dicotyledonous plants including Brassica [33], Ricinus [28], Momordica [27], Pisum [ 12], Arabidopsis [24] and Helianthus [31].…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis, cDNA and amino acid sequences of a precursor of conglutin ?, a sulphur-rich protein from Lupinus angustifolius

Gayler¹,

Kolivas²,

Macfarlane³

et al. 1990

Plant Mol Biol

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The biosynthesis of conglutin delta has been studied in developing cotyledons of Lupinus angustifolius L. Precursors of conglutin delta formed the major sink for [35S]-cysteine incorporated by developing lupin cotyledons, and these precursors were rapidly sequestered into the endoplasmic reticulum. The sequence of a cDNA clone coding for one such precursor of conglutin delta was determined. The structure of the precursor polypeptide for conglutin delta predicted from the cDNA sequence contained an N-terminal leader peptide of 22 amino acids directly preceding a subunit polypeptide of Mr 4520, together with a linking region of 13 amino acids and a subunit polypeptide of Mr 9558 at the C-terminus. The amino acid sequence predicted from the cDNA sequence showed minor variations from that established by sequencing of the protein purified from mature dried seeds (Lilley and Inglis, 1986). These were consistent with the existence of a multi-gene family coding for conglutin delta. Comparison of the sequences of conglutin delta with those of other 2S storage proteins showed that the cysteines involved in internal disulphide bridges between the mature subunits of conglutin delta, were maintained throughout this family of proteins but that little else was conserved either at the protein or DNA level.

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Occurrence of Low Molecular Weight and High Cysteine Containing Albumin Storage Proteins in Oilseeds of Diverse Species

Youle

Huang

1981

American J of Botany

135

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The proteins in the oilseeds of species from 11 families, including sunflower, mustard, linseed, almond, lupin, peanut, cucumber, Brazil nut, hazelnut, yucca, castor bean, and cottonseed were studied. Sucrose gradient centrifugation showed that a substantial proportion of the total seed protein from each species migrated with a 2S sedimentation coefficient. The 2S proteins, being water‐soluble and thus termed albumins, comprised 20–60% of the total seed proteins, while faster migrating globulins comprised the rest. The amino acid compositions of the 2S proteins were characterisitic of storage proteins by having a high amide content. However, the 2S proteins are different from the classical globulin storage proteins in having a high content of cysteine. 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. They play an additional and unique role of providing sulfur reserve for germination.

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IV. Amino acid composition of the globulins from Lupinus angustifolius and Lupinus luteus

Cited by 20 publications

References 8 publications

Lupin Globulins

Lupin Globulins

Biosynthesis, cDNA and amino acid sequences of a precursor of conglutin ?, a sulphur-rich protein from Lupinus angustifolius

Occurrence of Low Molecular Weight and High Cysteine Containing Albumin Storage Proteins in Oilseeds of Diverse Species

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