No description available.

No description available.

No description available.

The studies presented in this thesis represent an attempt to characterise some aspects of the abnormalities of somatomedin physiology in protein-energy malnutrition. A suitable bioassay to study somatomedin was found in that of Van den Brande and Du Caju (1974) which makes use of uniform discs of cartilage punched from slices of immature porcine costal cartilage. The handling of the cartilage discs was made easy by the specially designed incubation rack. Preincubation increased sensitivity of the cartilage, and post incubation with radioactive tracer reduced the potential interference of varying sulphate content of assay samples. Serum samples were subjected to formal multipoint parallel line bioassay and data analysed by a computer programme designed to examine such assays. The bioassay was found to be sensitive to a concentration of serum of 5% and to have an index precision of less than 0.30 (and usually less than 0.20).

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This study assessed aspects of targeting of the PEM scheme in Gauteng province. This food supplementation scheme targets beneficiaries including children 0-6 years, using largely anthropometric criteria. Routine provincial intervention data was analysed and related to available data cm expenditure, population and indices of socio-economic need. Only 28% were children in the critical 7-36 month age group; and coverage was very low, with no correlation between indices of need and programme implementation by area. An exit interview to a sample of caretakers of 0-6 year old children in four clinics (two Local Authority, two provincial) examined the process of identification of beneficiaries. Low attendance by children over 1 year and 40% errors in growth monitoring, more frequent among sick children, effectively reduced screening coverage among the most at-risk. Health worker misclassification resulted in an 81% exclusion error among those meeting entry criteria, while 4% of the total were wrongly enrolled. Advice and nutrition promotion to caregivers was inadequate. Recommendations include service re-organisation, community-based initiatives and better monitoring.

The purpose of the present investigation was to study the effect of prolonged protein-calorie malnutrition on intestinal disaccharidase activities and on disaccharide absorption, as carbohydrate intolerance is a major problem in children suffering from protein-calorie malnutrition. Four groups of rats (90 to 120 grams) were fed the following diets for 8 to 9 weeks: control (18% lactalbumin, 66% carbohydrate); low protein low carbohydrate (0.5% lactalbumin, 66% carbohydrate); low protein high carbohydrate (0.5% lactalbumin, 83.5% carbohydrate); and low protein restricted (1% lactalbumin, restricted to 4 grams per day). After 8.5 weeks, part of the group on the 0.5% lactalbumin low carbohydrate diet was fed the control diet (18% lactalbumin, 66% carbohydrate) for 8 weeks. At the end of the feeding period, the following assays were performed: 1) in vivo absorption of radioactive (¹⁴C) lactose, sucrose, and maltose; 2) activities of intestinal lactase, sucrase, and maltase; 3) plasma albumin concentrations; and 4) mucosal protein concentrations. In the three protein deficient groups (0.5% lactalbumin low carbohydrate, 0.5% lactalbumin high carbohydrate, and 1% lactalbumin), the activity of both the jejunal and ileal disaccharidases and the absorption of lactose, sucrose and maltose were significantly higher when compared with the controls. The jejunal sucrase and maltase activities were significantly higher in the 0.5% lactalbumin high carbohydrate group than in the 0.5% lactalbumin low carbohydrate group, but the absorption of lactose, sucrose and maltose were alike. When the 1% lactalbumin (restricted to 4 grams per day) and the 0.5% lactalbumin low carbohydrate groups were compared, there were no statistically significant differences in the specific activities of the intestinal disaccharidases or the absorption of the disaccharides. The absorption of lactose, sucrose, or maltose were similar in the controls and the protein repleted group. The disaccharidase activities were also similar in these two groups except for a significant depression of jejunal maltase and ileal sucrase and maltase activities in the protein repleted group. Therefore, these results indicate that protein deprivation in rats for 8.5 weeks causes an increase in specific activities of the intestinal disaccharidases in both the jejunum and ileum, and that these changes caused by protein depletion may be reversed by feeding a diet high in protein. Also, an increase in the carbohydrate content of the protein deficient diet results in an induction of jejunal sucrase and maltase activities. The high specific activity of the intestinal disaccharidases following protein-calorie malnutrition may be in part due to a preferential loss of structural proteins rather than to an increase in enzymatic protein in the intestinal mucosa. The increase in the disaccharidase activities in the protein deficient rats is accompanied by an increase in disaccharide absorption which could be due to the higher levels of disaccharidases or to an increase in the transport of the constituent monosaccharides. The demonstration of statistically significant differences in sucrase and maltase activities between the 0.5% lactalbumin high carbohydrate and the 0.5% lactalbumin low carbohydrate groups without a concomitant increase in sucrose and maltose absorption, supports the view that the higher absorption of sucrose and maltose in the protein deficient rats is a result of increased monosaccharide transport. The results of this study are not consistent with the suggestion that protein-calorie malnutrition is responsible for disaccharide intolerance in children. / Land and Food Systems, Faculty of / Graduate

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MTHFD is a folate-dependent trifunctional protein comprised of three activities: N$ sp5$,N$ sp{10}$-methylenetetrahydrofolate dehydrogenase, N$ sp5$,N$ sp{10}$-methenyltetrahydrofolate cyclohydrolase and N$ sp{10}$-formyltetrahydrofolate synthetase. The enzymes catalyse the sequential interconversion of tetrahydrofolate derivatives required for purine, methionine and thymidylate synthesis. A Chinese hamster ovary cell line, reported to have reduced cyclohydrolase activity, was studied to characterize the nature of its mutation. / Enzymatic assays showed reduced activities of all three enzymes. Immunoblotting and immunoprecipitation of radiolabelled cell extracts indicated that the gene product was greatly reduced or absent in the mutant. Southern analysis showed no differences between normal and mutant cells, indicating that the defect was not due to a major gene rearrangement. RNA analysis, by Northern blotting and by RNA amplification using the polymerase chain reaction, showed that a mRNA for MTHFD of normal size was present in mutant cells. These results suggest that the mutation is post-transcriptional and that it disrupts the synthesis of MTHFD.