Plant seed globulins

As with pH, proteins may vary in solubility as a function of temperature, and some are quite sensitive. One can take advantage of this property with both bulk and microtechniques (Jacoby, 1968 McPherson, 1999). Many of the earliest examples of protein crystallization were based on the formation of concentrated solutions at elevated temperatures followed by slow cooling. Osborne in 1892 successfully crystallized over 20 plant seed globulins by cooling relatively crude extracts from 60°C to room temperature in the presence of varying concentrations of sodium chloride. 

Marcone, M.F., Kakuda, Y., and Yada, R.Y. 1998. Salt-soluble seed globulins of dicotyleonous and monocotyledonous plants. II. Structural characterization. Food Chem. 63, 265-274. 

Marcone, M.F. Biochemical and biophysical properties of plant storage proteins a current understanding with emphasis on 1 IS seed globulins. Food Res. Int. 1999, 32, 79-92. 

Molecular modelUng strategies based on the use of small spheres have been extensively applied to systems not yet crystallized. The US globulins from plant seeds (rape, sunflower, soya, field bean, pea) of 3.0-3.6 X 10 and the 24S arthropod haemocyanins (crayfish, lobster) of M,. 9 X 10 are too large to be studied... 

Blood serum globulin, egg globulin, milk globulin and plant globulins, such as edestin from hemp seed and excelsin from Brazil nut, are related proteins from the sources indicated. 

QS, like those of other plants, store proteins in the embryo to provide nutrients for growth and development (Herman and Larkins, 1999). In the food area, proteins stored in seeds are the source of the proteins consumed directly as food by humans (Shewry et al., 1995). Stored proteins provide building blocks for rapid growth upon seed and pollen germination (Herman and Larkins, 1999). Osborne (1924) introduced a classification of plant proteins based on their solubility in a series of solvents, such as albumins in water, and globulins in saline. 

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