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An extracellular poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis.
Analysis of hydrolytic products of poly(3-hydroxybutyrate), several oligomeric esters of D(--)-3-Hydroxybutyric acid, and the methyl ester of the trimeric ester indicated that the enzyme hydrolyzed these substrates from the free hydroxyl terminus, releasing D(.--)-3,hydroxy butyrate dimer units one at a time.
Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis
Comparison of the deduced amino terminus with that obtained from sequence analysis of the purified protein indicated that poly(3-hydroxybutyrate) depolymerase exists as a 488-amino-acid precursor with a signal peptide of 27 amino acids, which is similar to that of A. faecalis T1.
Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerases from Pseudomonas lemoignei.
Degradation of poly(3-hydroxybutyrate) by poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1.
Contribution of Glutathione Peroxidase and Nitric Oxide to Potassium Bromate-Induced Oxidative Stress and Kidney Damage in Mice
The results suggest that reduction of cytoplasmic GPx activity resulted from the KBrO3 administration initiates oxidative stress and that NO also participates in the promotion of K BrO3-induced oxidative stressand kidney damage.
Polyphosphoinositides produced by phosphatidylinositol 3-kinase are poor substrates for phospholipases C from rat liver and bovine brain.
The ability of three pure types of bovine brain phospholipase C (PLC) and one pure rat liver PLC to utilize as substrates the recently discovered phosphatidylinositol 3-phosphate (PI-3-P), a putative phosphatids 3,4-bisphosphates ( PI-3, 4-P2), and phosphatide 3-kinase activities (PIP3) was investigated.
An extracellular D(-)-3-hydroxybutyrate oligomer hydrolase from Alcaligenes faecalis.
A third type of nucleoside diphosphate kinase from spinach leaves: purification, characterization and amino-acid sequence.
Contribution of nitric oxide to potassium bromate-induced elevation of methaemoglobin concentration in mouse blood.
- Satoshi Watanabe, Shin-ichi Togashi, T. Fukui
- Chemistry, MedicineBiological & pharmaceutical bulletin
- 1 October 2002
KBrO3-induced methaemoglobinemia results from the reduction of GPx activity in blood by the KBrO2-induced increases in superoxide, NO and ONOO-.