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At least 883 records · Page 49Linked to original sources
PubMed2002

Suspended particle adhesion on aquatic plant surfaces: implications for 137Cs and 133Cs uptake rates and water-to-plant concentration ratios.

Suspended particle adhesion on aquatic biota can significantly increase the apparent concentration of radionuclides above their endogenous value, leading to an overestimation of the uptake rate and concentration ratios. This study is an attempt to assess quantitatively the importance of suspended particle adhesion on periphyton samples (biological material coating submerged surfaces). The concentrations of 137Cs and stable Cs (133Cs) in periphyton, suspended particles and filtered water were measured to determine the net water-to-periphyton concentration ratios for 137Cs and stable Cs. The net amount of 133Cs (or 137Cs) taken up by periphyton was calculated by subtracting from the total amount of 133Cs (or 137Cs) on the collected material (periphyton + inorganic particles), the 133Cs (or 137Cs) due to the inorganic particles adhering to periphyton. The mass of suspended particles adhering to the periphyton surface was calculated using scandium as an indicator of the mineral fraction of the suspended particles. The relationship between the concentration ratios for 137Cs and stable Cs and suspended particle adhesion on periphyton external surfaces is discussed.

Cesium Radioisotopes↗
PubMed1975

Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi.

The properties of the homogeneous cutinase I, cutinase II, and the nonspecific esterase isolated from the extracellular fluid of cutin-grown Fusarium solani F. pisi (R.E. Purdy and P.E. Kolattukudy (1975), Biochemistry, preceding paper in this issue) were investigated. Using tritiated apple cutin as substrate, the two cutinases showed similar substrate concentration dependence, protein concentration dependence, time course profiles, and pH dependence profiles with optimum near 10.0. Using unlabeled cutin, the rate of dihydroxyhexadecanoic acid release from apple fruit cutin by cutinase I was determined to be 4.4 mumol per min per mg. The cutinases hydrolyzed methyl hexadecanoate, cyclohexyl hexadecanoate, and to a much lesser extent hexadecyl hexadecanoate but not 9-hexadecanoyloxyheptadecane, cholesteryl hexadecanoate, or hexadecyl cinnamate. The extent of hydrolysis of these model substrates by cutinase I was at least three times that by cutinase II. The nonspecific esterase hydrolyzed all of the above esters except hexadecyl cinnamate, and did so to a much greater extent than did the cutinases. None of the enzymes hydrolyzed alpha- or beta-glucosides of p-nitrophenol. p-Nitrophenyl esters of fatty acids from C2 through C18 were used as substrates and V's and Kms were determined...

Binding Sites↗
PubMed1991

Pectin methylesterase, metal ions and plant cell-wall extension. Hydrolysis of pectin by plant cell-wall pectin methylesterase.

The hydrolysis of p-nitrophenyl acetate catalysed by pectin methylesterase is competitively inhibited by pectin and does not require metal ions to occur. The results suggest that the activastion by metal ions may be explained by assuming that they interact with the substrate rather than with the enzyme. With pectin used as substrate, metal ions are required in order to allow the hydrolysis to occur in the presence of pectin methylesterase. This is explained by the existence of 'blocks' of carboxy groups on pectin that may trap enzyme molecules and thus prevent the enzyme reaction occurring. Metal ions may interact with these negatively charged groups, thus allowing the enzyme to interact with the ester bonds to be cleaved. At high concentrations, however, metal ions inhibit the enzyme reaction. This is again understandable on the basis of the view that some carboxy groups must be adjacent to the ester bond to be cleaved in order to allow the reaction to proceed. Indeed, if these groups are blocked by metal ions, the enzyme reaction cannot occur, and this is the reason for the apparent inhibition of the reaction by high concentrations of metal ions. Methylene Blue, which may be bound to pectin, may replace metal ions in the 'activation' and 'inhibition' of the enzyme reaction. A kinetic model based on these results has been proposed and fits the kinetic data very well. All the available results favour the view that metal ions do not affect the reaction through a direct interaction with enzyme, but rather with pectin.

Calcium↗