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1.
Artículo en Inglés | IMSEAR | ID: sea-167256

RESUMEN

Patients with impaired glucose tolerance (IGT) are now considered as being pre-diabetic, which indicates their relatively high risk for developing diabetes mellitus associated with abnormal metabolic syndrome and cardiovascular diseases. However, dietary modification and physical exercise may play a critical role in this respect. To determine the influence of dietary modification and physical exercise in subjects with impaired glucose tolerance in Bangladesh, thirty three newly detected otherwise healthy subjects with IGT, aged 30-63 years, were randomly selected to participate in a 12 weeks diet and exercise program. Substantial improvement in glucose tolerance was observed at the end of 12 weeks particularly in middle aged subjects (41-50 years). Mean fasting blood glucose and 2 hr post load glucose value were reduced significantly. Glucose tolerance was reverted to normal in 66.7% of the participants, remained unchanged in 26.7% and deteriorated to diabetes in 6.7%. Significant reduction in serum total cholesterol, LDL cholesterol along with mild deterioration in HDL cholesterol and increase in triglyceride values were observed. It was found that the principles of 'prudent diet' in combination with physical exercise are highly effective in improving glucose tolerance, lowering total cholesterol and LDL cholesterol in IGT subjects.

2.
Artículo en Inglés | IMSEAR | ID: sea-167248

RESUMEN

Peroxidase enzyme was isolated and purified from the pulp of disease infected ripen papaya of local variety by 90% ammonium sulphate precipitation, chromatography on DEAEcellulose followed by hydrophobic chromatography on Phenyl Sepharose CL-4B and the purifications achieved was about 7.2 fold with 2.5% recovery. The purified enzyme was homogeneous as judged by polyacrylamide slab gel electrophoresis. The purified enzyme had a Mr of about 55,000 and 50 000 as determined by gel filtration on Sephadex G-100 and SDS-PAGE, respectively. The molecular mass of the enzyme was found to be very similar under both reducing and non-reducing conditions indicating that the enzyme contains no subunit. The enzyme has the following characteristics: pH optima at 6.0, temperature optima around 38°C, enzyme activity was found to be strongly inhibited in the presence of potassium cyanide and Fe+2 while the activity was found to be remarkably increased in the presence of ammonium sulphate. The Km value for the peroxidase obtained with pyrogallol as substrate was 0.027 mM.

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