In-Water Resisted Swim Training for Age-Group Swimmers: An Evaluation of Training Effects.

Purpose: The purpose of this study is to compare the efficacy of resisted sprint swim training with that of nonresisted sprint swim training on 50-m freestyle competition time (V50) in age-group swimmers.

Methods: Twenty-four age-group swimmers (age 10.6-14.

Regions of FtsZ important for self-interaction in Staphylococcus aureus.

Since FtsZ is structurally similar to eukaryotic tubulin, selective regions of S. aureus FtsZ have been swapped with equivalent regions from tubulin. These mutant FtsZ proteins were analyzed for their interaction with both wildtype FtsZ and FtsA using the yeast two-hybrid assay.

Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid.

The structure of the trimeric, manganese metalloenzyme, rat liver arginase, has been previously determined at 2.1-A resolution (Kanyo, Z. F.

Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ.

The essential bacterial cell division protein FtsZ (filamentation temperature-sensitive protein Z) is a distant homologue to the eukaryotic cytoskeletal protein tubulin. We have examined the GTP hydrolytic activity of Escherichia coli FtsZ using a real-time fluorescence assay that monitors phosphate production. The GTPase activity shows a dramatic, nonlinear dependence on FtsZ concentration, with activity only observed at enzyme concentrations greater than 1 microM.

L-arginine binding to liver arginase requires proton transfer to gateway residue His141 and coordination of the guanidinium group to the dimanganese(II,II) center.

Rat liver arginase contains a dimanganese(II,II) center per subunit that is required for catalytic hydrolysis of l-arginine to form urea and l-ornithine. A recent crystallographic study has shown that the Mn2 center consists of two coordinatively inequivalent manganese(II) ions, MnA and MnB, bridged by a water (hydroxide) molecule and two aspartate residues [Kanyo et al. (1996) Nature 383, 554-557].