isooctane/potato

Potato acid phosphatase, AcPase (E.C. 3.1.3.2) was entrapped in reverse micelles of cationic surfactant cetyltrimethylammonium bromide (CTAB) in isooctane and chloroform (1:1). The activity was studied at different values of Wo = ([water]/[surfactant]). AcPase exhibited superactivity in the reverse

Lipid acyl hydrolase (LAH; patatin) was purified from potato tubers by ammonium sulfate fractionation followed by anion-exchange and affinity chromatography. The major protein band of 40-43 kDa on SDS-PAGE appeared to be patatin, and it stained positive for lipase activity on native PAGE.

Patatin is a family of glycoproteins that accounts for 30-40% of the total soluble protein in potato (Solanum tuberosum L.) tubers. This protein has been reported not only to serve as a storage protein but also to exhibit lipid acyl hydrolase (LAH) activity. In this study patatin is characterized in

A simple and efficient method is presented for the extraction, cleanup, and liquid chromatographic (LC) determination of linuron and 3 of its metabolites, 3-(3,4-dichlorophenyl)-1-methyl urea (DCPMU), 3-(3,4-dichlorophenyl) urea (DCPU), and 3,4-dichloroaniline (DCA), in potatoes. Samples are

A sensitive and rugged residue analysis method was validated for the estimation of dithiocarbamate fungicides in a variety of fruit and vegetable matrices. The sample preparation method involved reaction of dithiocarbamates with Tin(II) chloride in aqueous HCl. The CS2 produced was absorbed into an