Abstract
Polyadenylated mRNA was isolated from germinating watermelon cotyledons and translated in a wheat germ protein synthesizing system. The synthesis of glyoxysomal malate dehydrogenase was detected by direct immunoprecipitation and electrophoretic analysis of the precipitate. In addition to a small amount of the authentic isoenzyme (subunit molecular weight = 33 000), the major part of the incorporated [35S] methionine was observed in a polypeptide with a molecular weight of 38 000. The possible role of the larger molecule as a precursor of glyoxysomal malate dehydrogenase is discussed.
Original language | English |
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Pages (from-to) | 636-643 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 81 |
Issue number | 2 |
DOIs | |
State | Published - 30 Mar 1978 |
Externally published | Yes |