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العنوان
Electrophoretic and biochemical studies on oil seed proteins /
المؤلف
Mostafa, Abd-El-Zaher Mohamed A.
هيئة الاعداد
باحث / عبد الظاهر محمد أبا صيرى مصطفى
مشرف / محمد نبيه الشوربجى
مناقش / رضا حلمى سمور
مناقش / عاطف محمد ابو شادى
الموضوع
Botany.
تاريخ النشر
1992.
عدد الصفحات
95 p. :
اللغة
الإنجليزية
الدرجة
ماجستير
التخصص
علوم النبات
تاريخ الإجازة
1/1/1992
مكان الإجازة
جامعة طنطا - كلية العلوم * - Botany
الفهرس
Only 14 pages are availabe for public view

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from 200

Abstract

Seeds and grains are the plant organs which have global interest as they are the main source of foods for both man and animals. In addition to their nutritional value, their proteins are conservative and reflectinq the genetic history of the plant species. Seed proteins include in addition to the storage proteins, housekeeping proteins, protease inhibitors, lectins and allergens. Some of the housekeeping proteins play an important role in food industry. Protease inhibitors, lectins, and allergens are very harmful to both man and animal. The study and biochemical characterization of seed proteins which is the backbone of this thesis is very important for improvinq the quality of the seed proteins through a traditional breeding and gene manipulation by using genetic engineering techniques. The mobilization of storage proteins during germination which is one of the aims of this study, is very important, since it will help in understanding how the seed proteins are digested and which enzymes play the key role in this process. In this thesis, the seed proteins of flax, sunflower and cotton were electrophoretically studied using PAGE, SDS-PAGE, PoroPAGE, SDS-PoroPAGE , IEF, Two-Dimensional gel/ME, and SDS-mapping. It was found that the major fraction of the globulin of both sunflower and flax seeds is legumin-like protein. On the contrary, the seed protein of cotton was very poor in disulphide-bonded proteins. Extraction of the seed proteins of sunflower and flax with either SDS or Urea inflects partial dissociation on their proteins. IEF and SDS-mapping showed that the globulin proteins of sunflower and flax are highly heterogeneous, indicating that proteins bands shown on SDS-PAGE are genetically controlled with large families of genes.