A contribution to the standardization of methods for the preparation of seed proteins ofAllium cepa L.
- 1 July 1979
- journal article
- research article
- Published by Institute of Experimental Botany in Biologia plantarum
- Vol. 21 (4) , 284-290
- https://doi.org/10.1007/bf02902211
Abstract
The study of certain conditions for the extraction of seed proteins ofAllium cepa revealed that the best extractibility of proteins is obtained by the use of a buffered physiological solution at 20 °C in comparison with TRIS-glycine buffer at 5 °C. Using potassium phosphate buffer with 0.01 M mercaptoethanol and 0.4 M NaCl, an amount of proteins by up to 25 per cent higher passes into solution as compared with the physiological solution, but these extracts are unsuitable for the electrophoretic separation in polyacrylamide gels. The defatting of the seed meal under low temperature did not affect the qualitative composition of the protein complex studied, the addition of a 1 per cent soluble starch to the polyacrylamide gel. improved its resolution.Keywords
This publication has 8 references indexed in Scilit:
- Studies on the Determination of Species and Cultivars on the Basis of Electrophoretic Patterns of Seed Protein and Seed EnzymesEngei gakkai zasshi (Journal of the Japanese Society for Horticultural Science), 1977
- Atypical composition of seed proteins in cultivars ofPhaseolus vulgaris L.Biologia plantarum, 1976
- PURIFICATION AND PHYSICO‐CHEMICAL PROPERTIES OF 11S GLOBULIN IN SOYBEAN SEEDSInternational Journal of Peptide and Protein Research, 1972
- Immunochemical Studies on Arachis hypogaea Proteins With Particular Reference to the Reserve Proteins. I. Characterization, Distribution, and Properties of α-Arachin and α-ConarachinPlant Physiology, 1969
- Enzym-Elektrophorese in Einschluß-Polymerisaten des Acrylamids. A. Amylasen, PhosphorylasenZeitschrift für Naturforschung B, 1967
- ENZYM-ELEKTROPHORESE IN EINSCHLUSS-POLYMERISATEN DES ACRYLAMIDS .A. AMYLASEN PHOSPHORYLASEN1967
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Purification and characterization of the 11S component of soybean proteinsArchives of Biochemistry and Biophysics, 1959