Energy expenditure of obese, overweight, and normal weight females during lifestyle physical activities.

Objective: To quantify energy expenditure of various lifestyle physical activities of obese, overweight, and normal-weight girls.

Methods: In total, fifty-five girls participated in six activities: a treadmill walk at 4.0 km x hr(-1), run, football throw, walk in open area, cycle, and riding a scooter.

Invertase storage stability and sucrose hydrolysis in solids as affected by water activity and glass transition.

Research continues to differentiate the impact of water activity (a(W)) and the glass transition temperature (T(g)) on chemical reactions. Invertase with and without sucrose was incorporated into low and high molecular weight poly(vinylpyrrolidone) model systems (PVP-LMW and PVP-K30, respectively). Invertase activity and sucrose hydrolysis were monitored during storage at a(W) = 0.

Ligand-induced conformational changes of thymidylate synthase detected by limited proteolysis.

Limited tryptic proteolysis was used to investigate conformational changes of thymidylate synthase from Lactobacillus casei induced by ligand binding. Most of the identified sites of proteolysis were between R72 and R178, a region that includes a large loop containing residues 90-139 that is absent in thymidylate synthase from most other sources. Hydrolysis at both ends of this region was affected by the presence of dUMP.

Interaction of pyridoxal phosphate with thymidylate synthase: spectral and equilibrium dialysis studies.

1. Changes in the spectrum of pyridoxal phosphate (PLP) were produced by adding an equimolar amount of native thymidylate synthase, but not by adding denatured enzyme or enzyme modified by sulfhydryl-blocking reagents. 2.

Enzyme selectivity analyses of arylsulfonylamino acid aldose reductase inhibitors.

Arylsulfonylamino acids, displaying a wide range of inhibitory activities versus rat lens aldose reductase (RLAR), were analyzed for enzyme selectivity in several test systems. These RLAR inhibitors were found not to produce significant inhibition of genetically-linked reductases (aldehyde reductase, ALR), catalytically similar reductases (Pachysolen tannophilus xylose reductase, PTXR), functionally distinct oxidoreductases (glutathione reductase, GR, lactate dehydrogenase, LDH, and gamma-transaminase, GABA-T), and thymidylate synthase (TS). These data suggest that aldose reductase differs significantly from other oxidoreductases in its inhibitor binding domain(s).