The comparison of lectin spectra of certain representatives of the speciesPhaseolus vulgaris ssp.aborigineus of different geographical origin

Author:

Švachulová Jiřina,Klozvá Eva,Hadačová Věra,Turková Věra,Přikrylová Daniela

Publisher

Institute of Experimental Botany

Subject

Horticulture,Plant Science

Reference30 articles.

1. Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. - Anal. Biochem.72: 248–254, 1976.

2. Brown, J. W. S., Osborn, T. C., Bliss, F. A., Hall, T. C.: Bean lectins. Part 1. Relationships between agglutinating activity and electrophoretic variation in the lectin - containing G/2 albumin seed proteins of French bean (Phaseolus vulgaris L.). - Theor. appl. Genet.62: 263 to 271, 1982a.

3. Brown, J. W. S., Osborn, T. C., Bliss, F. A., Hall, T. C.: Bean lectins. Part 2. Relationship between qualitative lectin variation inPhaseolus vulgaris L. and previous observations of purified bean lectins. - Theor. appl. Genet.62: 361–367, 1982b.

4. Brücher, O.: Absence of phytohemagglutinin in wild and cultivated beans from South America. - Proc. trop. Region amer. Soc. bort. Sci.12: 68, 1968.

5. Brücher, O., Wecksler, A., Levy, A., Palozzo, W., Jaffé, G.: Comparison of phytohemagglutinins in wild beans (Phaseolus vulgaris) and their inheritance. - Phytochemistry8: 1739 to1743, 1969.

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