Functional and biochemical properties of proteins from safflower seed.
There are relatively few studies on the properties of proteins that comprise a major part of the safflower seed. The biochemical and functional properties of these proteins have not been fully discovered. In this study, safflower seed proteins were obtained by isoelectric precipitation in two fractions. One of the fractions (Fraction-1) was obtained at pH 10 and the other fraction was obtained, as the protein supernatant separate from the pH precipitate, by ultra filtration (Fraction-2). Functional and biochemical properties of both of fractions were investigated. Gel permeation chromatography (GPC) was applied to both fractions. GPC shows that high-molecular weight constituents are present only in fraction 1, whereas fraction 2 consists of proteins with lower molecular weights in comparison with protein standards. Sodium dodecyl sulfate polyacrylamide gel (SDS-PAGE) electrophoresis in the presence of mercaptoethanol and SDS with protein weight markers was applied to both of the fractions. The proteins in both of the fractions were separated and stained with Commassie Brillant blue R-250 dye on the PAGE gel. The molecular weight (M(w)) of each protein band was determined graphically by plotting Log M(w) and relative mobilities (R(f)) using GS-300 scanning densitometry and a suitable computer program.
Sagiroglu
Ayten
A
Department of Chemistry, Section of Biochemistry, Trakya University, Faculty of Science and Letters, Edirne, Turkey.
Ozcan
Hakki M
HM
Satana
Aziz
A
D031187:Carthamus tinctorius / Q000737:chemistry*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry*; D012995:Solubility
D010940:Plant Proteins