Author(s): Reda Helmy Sammour, M.N. El-Shourbagy, A.M. Abo-Shady and A.M. Abasary
Article publication date: 1995-12-01
Vol. 13 No. 3 (yearly), pp. 591-604.
159
Keywords
proteins, seeds, sunflower
Abstract
The seed proteins of sunflower (Helianthus annuus) were qualitatively and quantitatively investigated. Qualitative studies were carried out using different electrophoretic techniques (SDS-PAGE, Poro-PAGE, 2-D SDS-Page, Isoelectric focusing, Mapping gels). Analysis of the water extracted flour on SDS-Page and SDS-Poro-PAGE gave five major polypeptides with MWs of 63.5 KD, 60 KD, 58 KD, 55 KD and 51 KD. The pattern of the buffer extract exhibited 8 major polypeptides with MWs of 65.5 KD, 63.5 KD, 60 KD, 58 KD, 55 KD, 54 KD, 51 KD and 42.5 KD. Second dimension gel showed that the polypeptides with MWs of 65.5 KD, 60 KD, 58 KD, 55 KD, 54 KD, 51 KD are legumin-like proteins. Isoelectric points of the majority of the sunflower seed proteins were between 5 and 7 7. Mapping gels, however, showed that sunflower seed proteins were highly heterogeneous, especially the major bands. A quantitative study indicated that the albumin, globulin, prolamin and glutelin fractions amounted 38.32%, 39.04%, 5.53% and 17.09% respectively of the extracted proteins.