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Plant and Cell Physiology, 1970, Vol. 11, No. 4 579-588
© 1970


Article

Characterization of aspartate aminotransferase in germinating pumpkin cotyledon

WALTER E. SPLITTSTOESSER

Department of Horticulture, University of Illinois Urbana, Illinois 61801, U.S.A

During germination an increase in aspartate aminotransferase (E.C. 2.6.1.1 [EC] .) occurs in the cotyledons of pumpkin seedlings grown either in the light or dark with the bulk of the enzyme activity in the soluble fraction. The soluble and particulate enzymes had a pH optimum of 8.0, an {alpha}-ketoglutarate optimum of 0.02 mM and a broad aspartate optimum from 0.05 to 0.2 mM. The velocity of the reaction was proportional to the enzyme concentration over a wide range. The soluble enzyme was shown to require manganese and pyridoxal-5-phosphate and an active sulfhydryl group for maximum activitiy. The soluble enzyme was easily destroyed by pepsin while the particulate enzyme lost activity upon washing. It is suggested that aspartate aminotransferase plays a role in nitrogen metabolism during protein hydrolysis in germinating pumpkin cotyledons.

(Received January 6, 1970; )
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