[Electrophoresis of soluble alfalfa proteins (SDS) on polyactrilamide gel]
1988
Popovic, Z. (Poljoprivredni kombinat Beograd, PAdinska Skela (Yugoslavia). PKB-Agroekonomik) | Grujic-Ignjac, B. | Kolarski, D. | Vucetic, J. | Popovic, J. | Cirovic, M.
Investigation into the effect of different dehydration temperatures (40'C, 105'C, 650'C and 850'C) upon changes in the structure of alfalfa proteins proved the following: albumins, glubilins I and globulins II are not homogenous proteins and are composed of several subfractions; albumins of alfalfa dehydrated at temperatures of 40'C and 105'C are composed of all the 3 subfractions, A, B and C whereas albumins of alfalfa dehydrated at 650'C and 850'C have only the least mobile subfraction C, since subfractions A and B are very thermolabile and there appear denaturation and aggregation of the protein complex; globulins I of alfalfa dehydrated at temperatures of 40'C and 105'C are composed of subfractions, A, B and C whereas globulins I of alfalfa dehydrated at 650'C and 850'C are composed of subfractions B and C; proteins of the subfraction B are more stable at higher temperatures than the corresponding albumin fractions; alfalfa globulins II as compared with globulins I and albumins, have, at all dehydration temperatures, all the 3 subfractions, A, B and C which indicates that they are apparently more thermostable.
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