fluoride/potato

Finding appropriate adsorbent may improve the quality of drinking water in those regions where arsenic (As) and fluoride (F-) are present in geological formations. In this study, we evaluated the efficiency of potato peel and rice husk ash (PPRH-ash)-derived adsorbent for the removal of As and F

Pretreatment of discs excised from developing tubers of potato (Solanum tuberosum L.) with 10 millimolar sodium fluoride induced a transient increase in 3-phosphoglycerate content. This was followed by increases in triose-phosphate, fructose 1,6-bisphosphate and hexose-phosphate (glucose 6-phosphate

Alpha-D-Glucopyranosyl fluoride was found to inhibit strongly the action of alpha-glucan phosphorylase b[EC 2.4.1.1] from rabbit muscle, and that of the enzyme from potato tubers rather weakly. The inhibition is highly specific, being competitive with respect to glucose 1-phosphate and

The amount of fluoride present naturally in drinking water is highly variable, being dependent upon the individual geological environment from which the water is obtained. Chronic exposure to exceeding fluoride doses induces set of toxic effects, i.e. fluorosis. The aim of this study was to examine

The effects of fluoride on the activities of acid phosphatase (EC 3.1.3.2) from potato and alkaline phosphatase (EC 3.1.3.1) from E. coli during pyrophosphate and p-nitrophenylphosphate hydrolysis and on the activities of inorganic pyrophosphatase (EC 3.6.1.1) from baker's yeast during pyrophosphate

A study was conducted in fluoride-affected Bankura and Purulia districts of West Bengal to assess the potential health risk from fluoride exposure among children, teenagers, and adults due to consumption of rice, pulses, and vegetables in addition to drinking water and incidental ingestion of soil

Potato virus Y strain NN (PVYNN) was purified from mechanically infected plants Nicotiana tabaccum cv. Samsun by extraction of the plants with various buffers, clarification of the suspensions with chloroform or Triton X-100, high speed centrifugation of the virus through sucrose cushion and

The affinity constant Ka of PPi-PFK for Fru 2,6-P2 is equal to 1.56 nM for the potato enzyme and to 6.67 nM for that of the mung bean in the absence of chloride ions. These results are notably lower than the currently reported 5.5 nM and 30, 50 nM respectively. It is shown that the chloride ion is a

The role of the protein phosphorylation mechanism in the mobilization of vegetative storage proteins (VSPs) is totally unknown. Patatin is the major VSP of the potato (Solanum tuberosum L.) tuber that encompasses multiple differentially phosphorylated isoforms. In this study, temporal changes

The in vivo phosphorylation of starch was studied in Solanum tuberosum cv Dianella and Posmo. Small starch granules contain 25% more ester-bound phosphate per glucose residue than large starch granules. The degree of phosphorylation was found to be almost constant during tuber development. Isolated

The plasma membrane from the human tumor astrocytoma contains an active acid phosphatase activity based on hydrolysis of p-nitrophenyl phosphate. Other acid phosphatase substrates--beta-glycerophosphate, O-phosphorylcholine, and 5'-AMP--are not hydrolyzed significantly. The phosphatase activity is

Proteolytic cleavage in an exposed loop of human tartrate-resistant acid phosphatase (TRAcP) with trypsin leads to a significant increase in activity. At each pH value between 3.25 and 8.0 the cleaved enzyme is more active. Substrate specificity is also influenced by proteolysis. Only the cleaved

Crystalline, alpha-glucosidase-free sweet potato beta-amylase was found to catalyze hydration of the enolic bond of maltal (alpha-D-glucopyranosyl-(1----4)-2-deoxy-D-glucal) to form 2-deoxymaltose (alpha-D-glucopyranosyl-(1----4)-2-deoxy-D-glucose). The reaction at pH 5.0 showed Vmax 0.082

Skimmed camel milk contains 59,900 U/L amylase, which is 39,363 times less than serum and plasma amylase. Camel milk beta-amylase was purified as a 61 KDa band using DEAE-Sepharose and Sephadex G-100 and yielded 561 U/mg. The optimum working pH, Km and temperature were 7.0, 13.6 mg/Lstarch, 30-40

Tartrate-resistant acid phosphatase active on nucleoside di- and triphosphate substrates was isolated from developing rat bone and purified 2500-fold. The enzyme concentration had a purple coloration and activity that was sensitive to reducing agents. Mild reducing agents such as ferrous ion and