Purification, cloning, and characterization of the CEL I nuclease.

Recombinant nucleases CEL I from celery and SP I from spinach for mutation detection

BACKGROUND The detection of unknown mutations is important in research and medicine. For this purpose, a mismatch-specific endonuclease CEL I from celery has been established as a useful tool in high throughput projects. Previously, CEL I-like activities were described only in a variety of plants and could not be expressed in an active form in bacteria. RESULTS We describe expression of activ...

THE GENE CLONING, OVEREXPRESSION, PURIFICATION, AND CHARACTERIZATION OF DIBENZOTHIOPHENE MONOOXYGENASE AND DESULFINASE FROM GORDONIA ALKANIVORANS RIPI90A

The biodesulfurization (BDS) of sulfur compounds in fossil fuels is a process to reduce sulfur dioxide emissions that cause environmental pollution. Gordonia alkanivorans RIPI90A is able to convert dibenzothiophene, an organic sulfur compound in petroleum, to 2-hydroxybiphenyl (2-HBP) in 4S pathway. In this study, (DBT), DszA and DszB, DBT sulfone monooxygenase, and desulfinase were respectivel...

Detection, Cloning, Molecular Characterization and Phylogenic Analyses of a New Primate T-Cell Lymphotropic Virus Type I in Olive Baboon

Affinity Purification and Characterization of Recombinant Bacillus sphaericus Phenylalanine Dehydrogenase Produced by pET Expression Vector System

Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 (DE3). The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Re...

PURIFICATION AND PARTIAL CHARACTERIZATION O F PEROXIDASES FROM CULTIVATED RAPHANUS SATIVUS L. VAR. CICIL

Two peroxidases (EC. 1.11.1.7), POD I and POD II were purified from the roots of cultivatedRaphanus sativus L. Var. Cicil by one step ion-exchange chromatography after fractionation by acetone. The molecular weight of these enzymes were 43000 and 41000 Daltons and RZ 1.2 and 2.0 for POD I and POD II, respectively. Both enzymes consisted of a single polypeptide chain on SDS-PAGE. The maximum...