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Flax Seed Proteins Comparison by Various PAGE‐Techniques in Slabs
Author(s) -
Sammour R. H.
Publication year - 1988
Publication title -
journal of agronomy and crop science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.095
H-Index - 74
eISSN - 1439-037X
pISSN - 0931-2250
DOI - 10.1111/j.1439-037x.1988.tb00329.x
Subject(s) - cultivar , buffer (optical fiber) , tris , globulin , chemistry , polyacrylamide gel electrophoresis , chromatography , electrophoresis , botany , horticulture , biology , biochemistry , enzyme , computer science , telecommunications , immunology
Seed proteins of a number of Egyptian, French, and British cultivars of flax have been separately extracted with buffer, and water and buffer respectively, and analyzed by slab electrophoresis: PAGE, SDS‐PAGE, and poro‐SDS‐PAGE (22.5%–10%), and by PAGIF. The protein patterns were compared to find out the best method to differentiate between flax cultivars. The results of the water extracts and the residue extracted with Tris/borate buffer and analyzed on SDS‐PAGE indicated that the approximate MWs of native albumins and globulins ranged from 4.2 to 1.2 and 7.6 to 1.6 × 10 4 , respectively. It is also shown that SDS‐PAGE of globulins extracted with Tris/borate buffer are the method recommended for differentiation of flax cultivars. The data of the total proteins extracted with Tris/HCl buffer and analyzed on SDS‐PAGE under reducing and non‐reducing conditions exhibited 5 disulphide bonded bands which on reduction gave acidic subunits and basic subunits.