The phospholipase D (PLD) was purified from leaves of cabbage (
Brassica oleracea L. var.
capitata L.). The molecular weight of the enzyme was estimated as 87 and 73.5-kDa on SDS-PAGE and gel filtration using Superdex 200 HR 10/30 column. The transphosphatidylation capacity of cabbage PLD was shown to be higher than that of
Streptomyces chromofuscus PLD. Although cabbage PLD showed a single band,
Streptomyces chromofuscus PLD gave several bands on nondenaturing and denaturing PAGE. These results indicated that the cabbage PLD was a monomer protein, while the
Streptomyces chromofuscus PLD was hetero oligomer, having several types with different molecular weights. Furthermore, the cabbage PLD included the duplicated HxKxxxxD catalytic motifs in the molecule, but the
Streptomyces chromofuscus PLD did not. Previously, YAMANE
et al. reported that the transphosphatidylation capacity of
Streptomyces sp. PLD was higher than that of
Streptomyces chromofuscus. These results indicated that the high degree of the transphosphatidylation capacity of cabbage PLD was due to the existence of HxKxxxxD catalytic motifs.
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