Toxicological Characterization of Pesticide Residue in Phaseolus vulgaris
نویسندگان
چکیده
منابع مشابه
Glycosidases of Phaseolus vulgaris
The enzymes, cr-galactosidase, P-galactosidase, a-mannosidase, P-glucosidase, and p-acetylglucosaminidase, have been purified from the germinating seeds of Phaseolus vulgaris. All five enzymes have been simultaneously isolated in a highly active form. The pH optimum, K,,,, and energy of activation of each glycosidase for the reaction of hydrolysis of the appropriate P-nitrophenyl glycoside have...
متن کاملPurification and Characterization of Asparaginase from Phaseolus vulgaris Seeds
L-asparaginase from bacteria has been used in treatment of acute lymphoblastic leukemia. The aim of this study was to purify and characterize L-asparaginase from Phaseolus vulgaris seeds instead of microbial sources. L-asparaginase was purified to apparent homogeneity. The enzyme has molecular mass of 79 kDa. The purified asparaginase had very low activity toward a number of asparagine and glut...
متن کاملPurification and partial characterization of Phaseolus vulgaris seed aminopeptidase.
The aminopeptidase activity of Phaseolus vulgaris seeds was measured using L-Leu-p-nitroanilide and the L-aminoacyl-ss-naphthylamides of Leu, Ala, Arg and Met. A single peak of aminopeptidase activity on Leu-ss-naphthylamide was eluted at 750 microS after gradient elution chromatography on DEAE-cellulose of the supernatant of a crude seed extract. The effluent containing enzyme activity was app...
متن کاملPurification, characterization, and cDNA cloning of profilin from Phaseolus vulgaris.
Profilin from common bean (Phaseolus vulgaris L.) was purified to homogeneity by poly-L-Pro affinity chromatography and gel filtration. The hypocotyl and symbiotic root nodule protein was detected as a single isoform with a 14.4-kD molecular mass and an isoelectric point of 5.3. Partial amino acid and DNA sequencing of a full-length cDNA clone confirmed its identity as profilin. An antibody gen...
متن کاملOligosaccharide Specificities of Phaseolus vulgaris
The structural determinants required for interaction of oligosaccharides with leukoagglutinating phytohemagglutinin (L-PHA) and erythroagglutinating phytohemagglutinin (E-PHA) from Phaseolus vulgaris have been studied by immobilized lectin affinity chromatography. Homogeneous oligosaccharides of known structure, purified following release from Asn with Nglycanase and reduction with NaBH4, were ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Pakistan Journal of Biological Sciences
سال: 2020
ISSN: 1028-8880
DOI: 10.3923/pjbs.2020.1601.1606