Perceived and desired weight, weight related eating and exercising behaviours, and advice received from parents among thin, overweight, obese or normal weight Australian children and adolescents.

Background: Thin children are less muscular, weaker, less active, and have lower performance in measures of physical fitness than their normal weight peers. Thin children are also more frequently subjected to teasing and stigmatization. Little is known about thin children's weight perceptions, desired weight and attitudes and behaviours towards food and exercise.

Barriers to routine gynecological cancer screening for White and African-American obese women.

Background: Obese women are reported to be at higher risk from gynecological cancers than nonobese women, yet these women are less likely to get cancer-screening tests. The specific factors that contribute to obese women not obtaining timely cancer screening have not been identified.

Objective: To investigate the factors that contribute to lower rates of gynecological cancer screening as related to women's body size.

The National Weight Control Registry: a critique.

This article is a critique of the claim that the National Weight Control Registry provides data showing that a significant number of adults in the United States have achieved permanent weight loss. We believe that promoting calorie-restricted dieting for the purpose of weight loss is misleading and futile. We advocate the adoption of a health-at-every-size (HAES) approach to weight management, focusing on the achievement and maintenance of lifestyle changes that improve metabolic indicators of health.

Molybdate binding by ModA, the periplasmic component of the Escherichia coli mod molybdate transport system.

ModA, the periplasmic-binding protein of the Escherichia coli mod transport system was overexpressed and purified. Binding of molybdate and tungstate to ModA was found to modify the UV absorption and fluorescence emission spectra of the protein. Titration of these changes showed that ModA binds molybdate and tungstate in a 1:1 molar ratio.

Three-dimensional solution structure of the N-terminal receiver domain of NTRC.

NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Brünger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints.

Molybdenum accumulation in chlD mutants of Escherichia coli.

The content of molybdenum in wild-type and chlD cells was measured under a variety of growth conditions to determine if cells with a defective chlD gene were able to accumulate molybdenum. The chlD cells accumulated less molybdenum than wild-type cells did but concentrated molybdenum to a level at least 20-fold higher than the concentration in the culture medium. Molybdenum was present within spheroplasts of chlD cells and was not dialyzable.

Effect of dietary protein and methionine on sulfite oxidase activity in rats.

Sulfite oxidase catalyzes the oxidation of sulfite to sulfate. To investigate whether or not sulfite oxidase activity (EC 1.8.

Xanthine oxidase activity and immunologically detectable protein in the C57B1/6 mouse.

1. Xanthine oxidase (XO) was purified from livers of C57B1/6 mice. Antibodies generated against the purified protein were used in an immunoassay to measure total XO protein.

Effect of dietary protein and iron on the fractional turnover rate of rat liver xanthine oxidase.

Rat liver xanthine oxidase activity is regulated in response to dietary protein and iron. To investigate whether the change in activity was mediated by a change in the rate of protein degradation, we measured the fractional turnover rate using the double-isotope technique with [3H]- and [14C]leucine and calculated the apparent half-life of xanthine oxidase in rats fed diets containing either 20 or 5% casein with either 35 or 5 mg iron/kg diet. Under control conditions, xanthine oxidase had an apparent half-life of 4.

Regulation of xanthine oxidase activity and immunologically detectable protein in rats in response to dietary protein and iron.

To investigate the mechanism for changes in xanthine oxidase activity in response to dietary protein and iron, we fed rats diets containing 50, 20 or 5% casein with either normal iron (35 mg Fe/kg diet) or low iron (5 mg Fe/kg diet). Xanthine oxidase activity changed in liver and intestinal mucosa in response to protein and iron, but immunologically detectable xanthine oxidase protein did not change. When total liver RNA isolated from these rats was translated by a rabbit reticulocyte lysate, we found no difference in the amount of xanthine oxidase that was translated.

Molybdenum-sensitive transcriptional regulation of the chlD locus of Escherichia coli.

The chlD gene in Escherichia coli is required for the incorporation and utilization of molybdenum when the cells are grown with low concentrations of molybdate. We constructed chlD-lac operon fusions and measured expression of the fusion, Mo cofactor, and nitrate reductase activities under a variety of growth conditions. The chlD-lac fusion was highly expressed when cells were grown with less than 10 nm molybdate.

Effect of molybdenum-deficient and low iron diets on xanthine oxidase activity and iron status in rats.

We tested the hypothesis proposed by Topham, Woodruff and Walker that intestinal xanthine oxidase is important for iron absorption. We made weanling rats xanthine oxidase-deficient and measured their growth and iron status. There were no significant differences between control and xanthine oxidase-depleted rats in growth or iron absorption or a variety of measures of iron metabolism, except that xanthine oxidase-depleted rats accumulated nonheme iron in the liver.

Molybdenum cofactor in chlorate-resistant and nitrate reductase-deficient insertion mutants of Escherichia coli.

We examined molybdenum cofactor activity in chlorate-resistant (chl) and nitrate reductase-deficient (nar) insertion mutants and wild-type strains of Escherichia coli K-12. The bacterial molybdenum cofactor was assayed by its ability to restore activity to the cofactor-deficient nitrate reductase found in the nit-1 strain of Neurospora crassa. In the wild-type E.

Identification of the molybdenum cofactor in chlorate-resistant mutants of Escherichia coli.

Experiments were performed to determine whether defects in molybdenum cofactor metabolism were responsible for the pleiotropic loss of the molybdoenzymes nitrate reductase and formate dehydrogenase in chl mutants of Escherichia coli. In wild-type E. coli, molybdenum cofactor activity was present in both the soluble and membrane-associated fractions when the cells were grown either aerobically or anaerobically, with and without nitrate.

Repression of nitrate reductase activity and loss of antigenically detectable protein in Neurospora crassa.

Experiments were performed to determine whether conditions which cause the rapid loss of nitrate reductase activity in Neurospora crassa mycelia were accompanied by the loss of antigenically detectable nitrate reductase protein. When mycelia with nitrate reductase activity were transferred to ammonia media, there was a rapid loss in the reduced nicotinamide adenine dinucleotide-nitrate reductase activity plus the parallel loss of the reduced nicotinamide adenine dinucleotide-diaphorase and the reduced methyl viologen-nitrate reductase activities associated with the nitrate reductase. In addition, there was the loss of cross-reacting material to anti-nitrate reductase antisera that was concomitant with the loss of nitrate reductase activity.

Characterization of molybdenum cofactor from Escherichia coli.

Molybdenum cofactor activity was found in the soluble fraction of cell-free extracts of Escherichia coli grown aerobically in media supplemented with molybdate. Cofactor was detected by its ability to complement the nitrate reductase-deficient mutant of Neurospora crossa, nit-1, resulting in the vitro formation of nitrate reductase activity. Acid treatment of E.

Reactions of the Neurospora crassa nitrate reductase with NAD(P) analogs.

The assimilatory NADPH-nitrate reductase (NADPH:nitrate oxidoreductase, EC 1.6.6.

Purification and Characterization of the Nitrate Reductase from the Diatom Thalassiosira pseudonana.

THE ASSIMILATORY NITRATE REDUCTASE (NADH: nitrate oxidoreductase, E.C. 1.