Descriptive study of sledding injuries in Canadian children.

Objectives: (1) To describe the characteristics of sledding injuries presenting to a pediatric emergency department and (2) To describe the sledding environment that leads to childhood sledding injuries.

Setting: A pediatric hospital emergency department in Ottawa, Canada and identified sledding sites in the region.

Methods: All patients less than 18 years with sled related injuries were included.

Chemical modification of 3-HBA-6-hydroxylase by phenylglyoxal: kinetic and physicochemical studies on the modified enzyme.

The inactivation of 3-HBA-6-hydroxylase isolated from Micrococcus species by phenylglyoxal and protection offered by 3-HBA against inactivation indicate the presence of arginine residue at or near the substrate binding site. The loss of enzyme activity was time and concentration dependent and displayed pseudo-first order kinetics. A 'n' value of 0.

A sampling theorem for EEG electrode configuration.

An analytical tool to help in selecting the number of electrodes required for recording electroencephalogram (EEG) signals is presented. The main assumption made is that the scalp can be modeled as a hemispherical surface. The number of sensors required to sample a surface is derived by using a mean square error (MSE) measure to approximate the continuous potential functions on the hemispherical surface.

Identification of the active-site peptide of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus oryzae.

The non-oxidative decarboxylation of aromatic acids is a poorly understood reaction. The transformation of 2,3-dihydroxybenzoic acid to catechol in the fungal metabolism of indole is a prototype of such a reaction. 2,3-Dihydroxybenzoic acid decarboxylase (EC 4.

2,3-Dihydroxybenzoic acid decarboxylase from Aspergillus niger. A novel decarboxylase.

2,3-Dihydroxybenzoic acid decarboxylase, the last enzyme in the fungal metabolism of indole to catechol, catalyzes the non-oxidative decarboxylation of 2,3-dihydroxybenzoic acid to catechol. Unlike most other decarboxylases, this enzyme does not require a cofactor, underlining the importance of active-site residues in the reaction mechanism. Earlier studies from this laboratory [Kamath, A.