Abstract
The comparison of mitochondrial and glyoxysomal malate dehydrogenase (EC 1.1.1.37) from cotyledons of germinating watermelon (Citrullus vulgaris Schrad., cv. Kleckey's Sweet No. 6) by means of serological methods and peptide patterns revealed a high degree of homology. The N-terminal sequence analysis yielded a distinct presequence of eight or nine amino-acid residues, respectively, which is followed by an almost identical stretch of at least 20 amino-acid residues. A very similar domain has been recognized for mitochondrial malate dehydrogenase from porcine heart and yeast, and for Escherichia coli malate dehydrogenase.
Original language | English |
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Pages (from-to) | 555-558 |
Number of pages | 4 |
Journal | Planta |
Volume | 169 |
Issue number | 4 |
DOIs | |
State | Published - Dec 1986 |
Keywords
- Citrullus
- Isoenzyme
- Malate dehydrogenase (glyoxysomal and mitochondrial)
- N-terminal sequence analysis