The synthesis and structure of pea storage proteins
| العنوان: | The synthesis and structure of pea storage proteins |
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| المؤلفون: | Donald Boulter, John A. Gatehouse, Ronald R. D. Croy, Peter R. Shewry |
| المصدر: | Critical Reviews in Plant Sciences. 1:287-314 |
| بيانات النشر: | Informa UK Limited, 1984. |
| سنة النشر: | 1984 |
| مصطلحات موضوعية: | chemistry.chemical_classification, food.ingredient, Globulin, Protein subunit, food and beverages, Plant Science, Biology, Amino acid, chemistry.chemical_compound, Monomer, food, chemistry, Biochemistry, Vicilin, biology.protein, Storage protein, Legumin, Cotyledon |
| الوصف: | The seeds of pea, Pisum sativum L., like those of other legumes, accumulate proteins in their cotyledons during development. These proteins are mainly globulins, soluble in aqueous salt solutions at neutral pH; in keeping with their physiological storage role they are multimeric proteins readily rendered insoluble for deposition, and have high proportions of amide amino acids. They are degraded on germination of the seed to provide nutrients for the growing plant. The two major seed proteins in pea are legumin, a hexameric molecule (Mr ⋍ 380,000) where each monomer (Mr ⋍ 60,000) contains an “acidic”; (Mr ⋍ 40,000) and a “basic”; (Mr ⋍ 20,000) subunit linked by a disulphide bond, and vicilin, a trimeric molecule (Mr ⋍ 150,000) where each monomer (Mr ⋍ 50,000) may contain breaks in its polypeptide chain, giving rise to a variety of smaller subunits. Both these proteins are synthesised on polyribosomes bound to the endoplasmic reticulum in cotyledon cells and are transported from there to membrane‐enclosed p... |
| تدمد: | 1549-7836 0735-2689 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_________::76cd774b4d0097ca70d23202611944f9Test https://doi.org/10.1080/07352688409382182Test |
| رقم الانضمام: | edsair.doi...........76cd774b4d0097ca70d23202611944f9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15497836 07352689 |
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