[Incidence of lactose intolerance discerned in population studies in Poland].
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Biomedical subjects
Publications and source records attributed to J Socha.
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The evaluation of hepatic degradation of glycogen in patients with different chronic liver diseases was carried out on the basis of: a) specific activities of hepatic enzymes involved in catabolism of glycogen; b) level of glycogen in liver biopsies; c) concentration of glucose and cAMP in serum after the intravenous administration of glucagon. In 13 out of 35 patients investigated the activity of glucose-6-phosphatase was decreased to 14-50% of the control value. In the livers of 3 patients glycogen phosphorylase activity was decreased to 10% of the control value. In patients with the significantly low activities of hepatic glucose-6-phosphatase and phosphorylase a, however, normal catabolism of glycogen in the liver was observed, neither hypoglycemia nor abnormal glycogen storage in liver biopsies nor abnormal response to glucagon being found. In the group of patients with decreased and normal activities of glucose-6-phosphatase and phosphorylase a, biochemical parameters in the serum (i.e. markers of liver damage) were not detectable. Possible causes of the selective and asymptomatic decrease in the activities of glucose-6-phosphatase and phosphorylase a are discussed.
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The diagnosis of vasoactive intestinal poly-peptide-secreting tumor (VIPoma) was established in two boys on the basis of watery diarrhea with hypokalemia, elevated plasma levels of vasoactive intestinal polypeptide (VIP) (range of 55-94 pmol/L), and presence of a tumor of the left adrenal gland. Despite celiac angiography, VIP estimation in blood samples taken from different parts of the body, and exploratory laparotomy, localization of the tumor in one child in vivo was unsuccessful. In the other boy, computed tomography revealed a large tumor in the left adrenal gland. Following the removal of the tumor, diarrhea ceased, and 10 days after surgery, the plasma level of VIP was 5 pmol/L. Histologically, the tumors in the two boys were found to be ganglioneuromas. The diagnosis of VIPoma is simple but localization can be very difficult. Surgical removal of VIPoma is often rewarding.
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A simple chromatographic procedure with the use of modified cellulose-nitrate membrane strips, 80 x 40 mm, has been worked out for the rapid isotopic assay of cyclic AMP (cAMP) phosphodiesterase (EC 3.1.4.17) and 5'-AMP nucleotidase (EC 3.1.3.5) in crude extracts of various tissues from animals and plants. The assay is based on enzymatic conversion of the product to adenine, a relatively inert compound which, in contrast to cAMP and 5'-AMP, is strongly adsorbed by the cellulose-nitrate membrane. Due to this property rapid separation of adenine from the unconverted substrate (cAMP or 5'-AMP) is possible. Commercial 5'-nucleotidase and easily obtainable crude extract of adenosine nucleosidase from barley leaves are used as coupling enzymes for the phosphodiesterase assay. The assay of phosphodiesterase in 0.5-2 microliter of blood (10(-5) to 4.10(-5) units) has been demonstrated on several examples.
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