A comparative study of the insoluble storage proteins and the lectins of seeds of the Euphorbiaceae

Lalonde, Louise; Fountain, David W.; Kermode, Allison R.; Ouellette, Francis B.; Scott, Kelly; Bewley, J. Derek; Gifford, David J.

doi:10.1139/b84-225

Cited by 13 publications

(8 citation statements)

References 9 publications

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“…Their subunits are heterodimers made up of polypeptides with molec-ular weights of approximately 30 kDa and 20 kDa linked by disulfide bridges. This class of seed storage proteins is also found in some angiosperm seeds, such as those in the Euphorbiaceae and the Cucurbitaceae (O'Kennedy et al 1979, Lalonde et al 1984. The major insoluble proteins from white spruce megagametophytes probably belong to this class of seed storage protein.…”

Section: Discussionmentioning

confidence: 89%

The seed proteins of white spruce and their mobilization following germination

Gifford

Tolley

1989

Physiologia Plantarum

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Buffer‐soluble proteins that have subunit molecular weights, in the presence of sodium dodecyl sulphate (SDS), of 47, 31 and 27 kilodaltons (kDa) form the major storage proteins in the mature white spruce [Picea glauca (Moench) Voss] seed. These proteins were found mainly in the megagametophyte. but smaller amounts were identified in the embryo. Following the completion of germination, this reserve was rapidly hydrolyzed in both tissues and probably plays a major nutritional role in the germinated seed. Buffer‐insoluble proteins were also found in megagametophytes and embryos from the mature seed. These proteins were soluble in buffer only if SDS was present. Predominant in this class of proteins were several that have a subunit molecular weight and structure that is characteristic of seed crystalloid storage proteins; the subunits were shown to be heterodimers with polypeptide molecular weights in the 33 kDa to 37 kDa and 23.5 kDa to 25 kDa ranges. This reserve was rapidly hydrolyzed in the germinated seed. Storage protein hydrolysis was accompanied by a significant increase in the soluble amino acid pool in both megagametophytes and embryos. Cell‐free extracts of mature seed megagametophytes and embryos contained leucine‐naphthylamidase (leuNAase) activity. Following germination. this activity was maintained at a constant level in megagametophytes but increased substantially in embryos.

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Section: Discussionmentioning

confidence: 89%

The seed proteins of white spruce and their mobilization following germination

Gifford

Tolley

1989

Physiologia Plantarum

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“…However, the protein from castor bean was also soluble in 0.37 mol.L -1 NaCl (Youle and Huang, 1976) whereas the similar fraction from E. heterophylla was not, even using a more concentrated solution (0.87 mol.L -1 NaCl). According to Gifford and Bewley (1983) and Lalonde et al (1984) there are two major types within 11S globulins: those which are soluble in salt solutions (e.g., legumins) and those which require the addition of urea or SDS for total solubility (e.g., crystalloids). Thus the insoluble protein of E. heterophylla seed may be included in the second group of globulins.…”

Section: Resultsmentioning

confidence: 99%

“…The major bands of albumins exhibited molecular masses between 29.5 to 66 kDa and 20 to 22 kDa; salt-soluble globulins between 43 to 47 kDa, 31 to 36 kDa and 18 to 26 kDa; salt insoluble proteins ranged between 29 to 36 kDa and 18 to 20.5 kDa. Lalonde et al (1984) reported for the insoluble protein (reduced form) from seeds of several Euphorbiaceae, including E. heterophylla, the predominance of two groups of polypeptides (20 to 25 kDa and 29 to 35 kDa). The polypeptides between 20 to 25 kDa were not prominent in our insoluble fraction (Figure 8) but were present in the salt-soluble fraction.…”

Section: Resultsmentioning

confidence: 99%

Seed reserve composition and mobilization during germination and initial seedling development of Euphorbia heterophylla

Suda

Giorgini

2000

Rev. Bras. Fisiol. Veg.

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-Seed composition and reserve mobilization were investigated in wild poinsettia (Euphorbia heterophylla L.). Lipids, around 60% of seed dry mass, are the major reserve. Proteins, including albumins (49%), salt insoluble globulins (30%), salt-soluble globulins (21%) and prolamins (0.3%), comprise about a quarter of seed dry mass. Soluble sugars comprise about 3.6% of seed dry mass, sucrose being the predominant sugar. Starch was not detected in the endosperm of E. heterophylla. Lipid depletion starts after initial imbibition, and is completed between 72 and 96 hours. Protein fractions exhibit different degradation patterns, salt-soluble globulins being continuously degraded after the start of imbibition whereas salt insoluble fractions are degraded between 36 and 72 hours, and albumins between 60 and 84 hours. Globulin depletion is accompanied by an increase in free amino acids in the endosperm whereas intense albumin depletion is not. This result suggests that during albumin depletion there is a rapid transfer of amino acids to the growing embryo. Histochemical studies indicated that light accelerates protein degradation in the micropylar area of the seed. Soluble sugars increase in the embryo with no concomitant decrease in the endosperm, suggesting that sugars are mostly originated from the catabolism of lipids. ADDITIONAL INDEX TERMS:Weed, wild poinsettia, Euphorbiaceae, proteins, lipids, carbohydrates. COMPOSIÇÃO E MOBILIZAÇÃO DE RESERVA DA SEMENTE DEEuphorbia heterophylla DURANTE A GERMINAÇÃO E DESENVOLVIMENTO INICIAL DA PLÂNTULA RESUMO -A composição e a mobilização de reservas da semente de amendoim-bravo (Euphorbia heterophylla L.) foi investigada. Os lipídios constituem cerca de 60% da massa seca da semente, sendo o principal material de reserva. As proteínas constituem aproximadamente a quarta parte da massa seca da semente distribuídas entre as frações de albuminas (49%), globulinas insolúveis (30%), globulinas solúveis em solução salina (21% ) e prolaminas (0,3%). Os açúcares solúveis constituem cerca de 3,6% da massa seca da semente, sendo a sacarose o açúcar predominante. O amido não foi detectado no endosperma de E. heterophylla. A degradação dos lipídios inicia-se logo após a embebição inicial da semente sendo completada entre 72 e 96 horas. As frações protéicas têm diferentes padrões de degradação: as globulinas solúveis são continuamente degradadas após o início da embebição da semente, as globulinas insolúveis entre 36 e 72 horas e as albuminas entre 60 e 84 horas. A degradação das globulinas é concomitante com o aumento nos níveis de aminoácidos no endosperma, mas a degradação de albuminas não é. Esse resultado sugere que durante a degradação de albuminas ocorre uma rápida transferência de aminoácidos do endosperma para o embrião. Estudos histoquímicos indicaram que a luz acelera a degradação das proteínas na região micropilar da semente. Os açúcares solúveis aumentam no embrião sem uma concomitante diminuição no esdosperma, sugerindo que os açúcares são originados do catabolismo de l...

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“…It is reported that there exist two major types within 11S globulins: those are soluble in salt solutions (e.g. legumin) and those that require the presence of urea or SDS for total solubility (Gifford et al 1982;Lalonde et al 1984;Suda and Giorgini 2000). Typically, the major storage proteins of dicots are globulins, and those of monocots are prolamins and glutelins Fig.…”

Section: The Solubility Of Sspsmentioning

confidence: 99%

Characterization of olive seed storage proteins

2007

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At present little is known about olive seed storage proteins (SSPs). A better understanding of olive SSPs will be important for future biotechnology efforts. In the present study, we first developed a protocol relied on chloroform for preparing protein samples free of lipids from lipid-rich olive seeds. Then, we characterized olive SSPs by SDS-PAGE, N-terminal sequencing and immunoblot. Two smaller subunits (20 and 21.5 kD) of SSPs were purified to homogeneity and used for antibody production or N-terminal sequencing. N-terminal sequencing confirmed that major olive SSPs are 11S globulins. Moreover, the components and size distribution of SSPs are identical among several olive cultivars examined, suggesting that their synthesis is highly conserved in this species. Olive SSPs are soluble in aqueous alcohol, with limited solubility in water and dilute salt. Thus, despite their homology with globulins, olive SSPs are similar in solubility to prolamins and different from globulins in other dicot plants. Finally, the accumulation of olive SSPs during fruit maturation was examined. Our results revealed that the accumulation of SSPs is time-dependent and tissue-specific, and only 105 days after pollination (DAP), did individual components of SSPs synthesize substantially, and accumulate rapidly in large quantities over a short period of time. Our results suggest that a 36 kD protein is the precursor of olive SSPs, and 90-105 DAP seems to be a crucial transition period (from a precursor to mature subunits) for the accumulation of SSPs.

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A comparative study of the insoluble storage proteins and the lectins of seeds of the Euphorbiaceae

Cited by 13 publications

References 9 publications

The seed proteins of white spruce and their mobilization following germination

The seed proteins of white spruce and their mobilization following germination

Seed reserve composition and mobilization during germination and initial seedling development of Euphorbia heterophylla

Characterization of olive seed storage proteins

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