PHASEOLUS-COCCINEUS L STORAGE PROTEINS - EXTRACTION AND CHARACTERIZATION

被引:5
作者
BERNARDI, R
LUPI, MC
DURANTE, M
机构
[1] Department of Agricultural Plant Biology, Genetics Section, University of Pisa, Pisa, 56124
[2] Institute of Agricultural and Forestal Chemistry, The University, Gallina, Reggio Calabria, 89061, Piazza S. Francesco
关键词
D O I
10.1007/BF02890873
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Phaseolus coccineus storage globulins were extracted from mature cotyledons, purified and characterized. Three major proteins were separated. A component showing erythroagglutinating activity was thoroughly purified by thyroglobulin-Sepharose chromatography. The relative molecular masses of the three fractions are Mr = 330, 178, and 500 kDa as determined by polyacrylamide gel electrophoresis (PAGE). They correspond to the proteins found in other systems and classified as phytohaemagglutinin (PHA), vicilin and legumin, respectively. Electrophoretic analyses under denaturating conditions (SDS-PAGE) evidenced the major subunits for the three proteins. Isoelectrofocusing of the isolated proteins indicated a large heterogeneity for vicilin. © 1990 Kluwer Academic Publishers.
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页码:198 / 204
页数:7
相关论文
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