Seed storage proteins

A. M. Altschul and H. L. Wilcke, eds., NeiP Protein Foods, Vol. 5, Seed Storage Proteins, Academic Press, Inc., New York, 1985, 471 pp. 

The amino acid composition of storage proteins differs from that of the complete sprout [12, 13]. At least in the case of oilseed rape, alfalfa (Medicago sativa L.) and Camelina sativa, amino acids in the sprout are used mainly, either directly or indirectly, for the synthesis of the Rubisco proteins. Computer analysis shows that the amino acid composition of cruciferin and napin is completely different to the amino acid composition of Rubisco. This indicates that amino acids released from the seed storage proteins must be converted into other amino acids prior to Rubisco synthesis. 

Human creatine kinase -MM MAK33 IgGl Cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle s disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, A. thaliana A. thaliana 2S2 seed storage protein SP + 0.02-0.4% TSP of fresh leaf extract (10-12% TSP of intercellular fluid) 52... 

Limongelli G, Laghetti G, Perrino P, Piergiovanni AR (1996) Variation of seed storage protein in landraces of common bean (Phaseolus vulgaris L.) from Basilicata, Southern Italy. Plant Breed 119 513-516... 

Teuber, S.S. and W. R. Peterson. Systemic allergic reaction to coconut (Cocos nucifera) in 2 subjects with hypersensitivity to tree nut and demonstration of cross-reactivity to legu-min-like seed storage proteins new coconut and walnut food allergens. J Allergy Clin Immunol 1999 103(6) 1180-1185. 

Other therapeutic proteins produced in plants include leuenkephalin, a neuropeptide produced in B. napus and Arabidopsis as part of the seed storage protein 2S albumin. The peptide was proteolytically cleaved from the storage protein and recovered by high-performance liquid chromatography (HPLC). In addition, a biologically active form of the human... 

Lawrence, M.C., Izard, T., Beuchat, M., Blagrove, R.J., Colman, P.M. (1994). Structure of phaseolin at 2.2 A resolution. Implication for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. Journal of Molecular Biology, 238, 748-776. 

Makri, E., Papalamprou, E., Doxastakis, G. (2005). Study of functional properties of seed storage proteins from indigenous European legume crops (lupin, pea, broad bean) in admixture with polysaccharides. Food Hydrocolloids, 19, 583-594. 

Proteins were then dissolved in 20 mL of 0.125 M Tris-HCl, pH 7.4 containing 1% (m/v) CHAPS and the protease inhibitor cocktail, and treated with CPLL. With several variations from the standard treatments such as other complementary extractions from seeds, the use of urea-containing extraction buffer, and an additional peptide ligand library, the total number of detected gene products was quite large. Two hundred and thirty one unique proteins were found in the pulp (vs. 56 described previously) and 61 in the seeds (vs. only four reported by the literature). In the latter case, the presence of seed storage proteins, oleosins, and histones were detected in the pulp, a thaumatin-like protein, an allergenic protein also named Ole el3, was confirmed. 

Beyer, K., Bardina, L., Grishina, G., and Sampson, H.A. 2002. Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing Seed storage proteins as common food allergens. J Allergy Clin Immunol 110(1) 154-159. 

From the 11 epitopes tested, 3 appeared to be immunodominant. Hazelnut is known to cross-react with tree pollen and only little data exist on pollen-unrelated allergens causing hazelnut allergy. As one example, the cDNA of Cor a 9, an 11S globulin seed storage protein has been cloned, but no experimental data on sequential IgE-binding epitopes have been obtained (Beyer et al., 2002). 

Wang, F., Robotham, J.M., Teuber, S.S., Tawde, P., Sathe, S.K., and Roux, K.H. 2002. Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J Allergy Clin Immunol 110(1) 160—166. 

P-Conglycinin n/a 140-180 7S-Globulin <30b Seed storage protein, water... 

Miles, M.J., Carr, H.J., McMaster, T.J., I Anson, K.J., Belton, P.S., Morris, V., Field, J.M., Shewry, P.R., Tatham, A.S. 1991. Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. Proc Natl Acad Sci USA 88 68-71. 

Shewry, P.R., Napier, J.A., and Tatham, A.S. 1995. Seed storage proteins Structures and biosynthesis. Plant Cell 1 945-956. 

Aaron M. Altschul (ed.), New Protein Foods Volume 1, Technology, Part A—1974. Volume 2, Technology, Part B—1976. Volume 3, Animal Protein Supplies, Part A—1978. Volume 4, Animal Protein Supplies, Part B—1981. Volume 5, Seed Storage Proteins—1985. 

Shewry PR, Halford NG. Cereal seed storage proteins Structures, properties and role in grain utilization. J Exp Bot 2002 53 947-958. 

Lin et al. (15) showed that sunflower meal was superior to soybean and sunflower concentrates or isolates In emulsion capacity. McWatters and Cherry (9) compared select functional properties of defatted soybean, peanut, field pea, and pecan flours and showed that major seed storage proteins were important in emulsifying and foaming properties. Protein solubility was related to the quality of the emulsions and foams. Behavioral characteristics contributed by nonprotein components that occur naturally In the seeds, especially carbohydrates, were Implicated. 

---