PLANT PHYSIOLOGY · 1966 · 44 citations · 12 references
Life SciencesBiochemistryPlant BiologyEnzymologyPlant BiochemistryPlant-microbe InteractionsBacterial Pathogenesis In PlantsBacterial Plant PathogensBlight DiseasesEnzyme CharacterizationFoliar Bacterial DiseasesPlant EnzymesBacterial Leaf BlightBlight PathogenesisEsterase ActivityHydrolytic EnzymesPhosphatase Enzyme ActivityPhosphatasesPolyacrylamide Gel ElectrophoresisSodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis
Multiple forms of hydrolytic enzymes were demonstrated in extracts of healthy bean leaves (Phascolus vulgaris L.) and bean leaves infected with the halo blight organism [Pseudomonas phaseolicola (Burkh.) Dowson] by polyacrylamide disc electrophoresis. Bean leaves contained up to 4 acid phosphatase bands, 9 esterase bands active towards alpha-naphthyl acetate, and 7 esterase bands towards alpha-naphthyl butyrate. Only low or no activity was found for alkaline phosphatase, lipase, and aminopeptidase. Two artifacts are described which were observed with the lead phosphate method for acid phosphatase and the Tween method for demonstration of lipase. After infection with the halo blight organism the major acid phosphatase of the host increased during early and decreased at later infection stages. An acid phosphatase of bacterial origin with a more neutral pH optimum could be demonstrated in infected leaves. It is suggested that the bacterial acid phosphatase plays a role in uptake of metabolites by the pathogen. Several esterase bands decreased after infection. One host band with activity towards alpha-naphthyl butyrate increased. Also the pathogen showed an esterase band with high activity towards alpha-naphthyl butyrate.
12
Marvin M. Nachlas, Benito Monis, David S. Rosenblatt et al. · The Journal of Cell Biology · 1960 · 318 citations · Full text