A comparison of the storage protein (globulin) of eight species of Cucurbitaceae

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Abstract
The percentage of globulin from cotyledons of dormant seeds of eight species of the Cucurbitaceae family was similar. After 4 days of germination, the globulin fraction decreased with a concomitant increase in the water-soluble protein fraction. Small changes in total protein occurred. Sodium dodecyl sulfate – polyacrylamide gel electrophoresis showed that the globulins of the eight species were composed of high molecular weight proteins which were different. The subunit arrangement of the globulin suggests a tetramer structure with a molecular weight greater than 200 000. After4 days of germination, a heat-stable, water-soluble protein was produced from the globulin. When this protein was reduced with β-mercaptoethanol, followed by electrophoresis, two peptides with molecular weights of 18 500 and 20 000 were produced in each species. It was concluded that all of the globulins have the same basic structure in different subunit arrangements.