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Biomedical subjects

W Endres

Publications and source records attributed to W Endres.

At least 55 records · Page 3Linked to original sources
PubMed1987

Agarose gel isoelectrofocusing of UDP-galactose pyrophosphorylase and galactose-1-phosphate uridyltransferase. Developmental aspect of UDP-galactose pyrophosphorylase.

The uridine diphosphogalactose pyrophosphorylase activity has been determined in human adult and fetal tissues as well as blood of various ages by measurement of UDP-galactose production from gal-1-p and UTP. The highest activity was found from adult liver in which the specific activity was about 5% of the gal-1-p uridyltransferase activity. In general adult tissues had a somewhat higher activity than the corresponding fetal tissues except erythrocytes in which fetuses had a 5-10 times higher activity than adults. From normal blood the pyrophosphorylase activity in erythrocytes decreased with age, but in the case of galactosemia the decrease with age was not distinct. According to agarose gel isoelectrofocusing studies, at least two isozyme forms for UDP-galactose pyrophosphorylase exist with the activity bands between pH 6.0-6.15. The patterns of AGIF bands of pyrophosphorylase varied according to the age of the samples, suggesting the development of the isozyme forms of pyrophosphorylase to be age-dependent. Uridyltransferase, on the other hand, resolved into multiple bands between pH 5.1-5.6 on agarose gels and the patterns varied according to the variants but not to the age. Significance of the decrease in the pyrophosphorylase activity in erythrocytes with age as well as of the difference in AGIF bands between normal and the galactosemic were discussed with regard to the pathology of classical galactosemia.

Adolescent↗
PubMed1987

"Peripheral" tetrahydrobiopterin deficiency with hyperphenylalaninaemia due to incomplete 6-pyruvoyl tetrahydropterin synthase deficiency or heterozygosity.

Four patients in three families with "peripheral" tetrahydrobiopterin deficiency were investigated. They were characterized biochemically by a tetrahydrobiopterin-responsive hyperphenylalaninaemia, a high neopterin/biopterin ratio in urine and plasma, and normal or elevated concentrations of biopterin, homovanillic acid, and 5-hydroxyindole acetic acid in cerebrospinal fluid. From measurements of the activity of erythrocyte 6-pyruvoyl tetrahydropterin synthase (PTS, formerly called phosphate-eliminating enzyme) and phenylalanine loading tests in the patients and their parents, one patient was demonstrated to be heterozygous for PTS deficiency. The others were obviously genetic compounds (allelism) with incomplete PTS deficiency. Three of the children developed normally, two of them under treatment with tetrahydrobiopterin. In the latter two patients, significantly lower concentrations of biopterin, homovanillic acid, and 5-hydroxyindole acetic acid in cerebrospinal fluid were noted at age 7 months (when treatment was interrupted) than those observed at 3 and 5 weeks, respectively. The infant who is heterozygous for PTS deficiency was born small for gestational age and showed a moderately delayed psychomotor development. It is concluded that "peripheral" tetrahydrobiopterin deficiency is caused by a partial PTS deficiency with sufficient activity to cover the tetrahydrobiopterin requirement of tyrosine 3-hydroxylase and trytophan 5-hydroxylase in brain but not enough for phenylalanine 4-hydroxylase in liver. For therapy, tetrahydrobiopterin, 2-5 mg/kg in a single oral dose per day, is recommended to keep plasma phenylalanine normal. A careful observation of the mental development is indicated.

Alcohol Oxidoreductases↗
PubMed1987

[Oxidative degradation of linoleic acid methyl ester in suspensions of inorganic excipients. 1. Auto-oxidation in the presence of silicic acid products and aluminum oxide].

Linoleic acid methyl ester (LME) was selected as a model to study the autoxidation of unsaturated compounds at the surfaces of inorganic excipients. From IR spectra of LME-silica adsorbates it was concluded that the interaction between LME and the silica surface is mainly due to hydrogen bonds, established between the ester carbonyl and the silica silanol groups. The autoxidation was continuously monitored by measuring the oxygen consumption of LME under UV light exposure and isobaric conditions, and, in parallel, by determining the carbonyl and peroxide values of LME. The oxidative degradation of LME is enhanced by porous and colloidal silicas as well as by colloidal aluminium oxide. From the oxygen consumption and the ratio of intermediates (carbonyls, peroxides) formed during the degradation of LME it was concluded that the prooxidative effect of the inorganic excipients can be attributed to an accelerated reaction of the peroxides of LME.

Aluminum↗
PubMed1987

Increased concentrations of HbAlab in hereditary fructose intolerance and galactosemia.

In patients with diabetes mellitus nonenzymatic glycosylation of hemo-globin is a result of increased blood glucose concentrations. In analogy glycosylated hemo-globin fractions were determined in 23 patients with hereditary fructose intolerance (HFI) and 8 patients with galactosemia (G) by means of hemoglobin chromatography on a column packed with Bio-Rex 70 resin. The concentrations were compared to those of 14 control patients and 43 patients with type 1 diabetes mellitus. Compared to controls, in HFI- and G-patients HbAlab was significantly increased. In contrast diabetic patients presented with a marked and significant increase of the HbAlc fraction. When purified hemoglobin was incubated with different monosaccharides respectively monosaccharide phosphates, an increase of HbAlab resulted mainly after galactose and fructose-1-phosphate. The determination of HbAlab in patients with HFI and G is considered a possible means of metabolic control.

Carbohydrate Metabolism, Inborn Errors↗
PubMed1986

Excitatory amino acids and intracellular pH in motoneurons of the isolated frog spinal cord.

Double-barrelled pH-sensitive micro-electrodes were used to measure changes of intracellular and extracellular pH in and around motoneurons of the isolated frog spinal cord during application of excitatory amino acids. It was found that N-methyl-D-aspartate, quisqualate and kainate produced a concentration-dependent intracellular acidification. Extracellularly, triphasic pH changes (acid-alkaline-acid going pH transients) were observed during the action of these amino acids. The possible significance of such pH changes for the physiological and pathophysiological effects of excitatory amino acids are discussed.

2-Amino-5-phosphonovalerate↗
PubMed1986

Changes in extracellular pH during electrical stimulation of isolated rat vagus nerve.

Double-barrelled pH-sensitive micro-electrodes were used to record changes of extracellular pH during repetitive stimulation of isolated rat vagus nerves. It was found that a small initial alkaline shift was followed by a prolonged acidification. The acidification was correlated in time with the poststimulus undershoot of the extracellular K+ activity and with the recovery phase of the nerve conduction velocity. In the presence of ouabain, the acid component of the pH change was completely abolished (indicating a metabolic origin), whereas the alkaline component remained unaltered. These pH changes were too small to make a significant contribution to the activity-related changes in conduction velocity of the vagal C-fibres.

Animals↗
PubMed1986

First trimester diagnosis of Pompe's disease (glycogenosis type II) with normal outcome: assay of acid alpha-glucosidase in chorionic villous biopsy using antibodies.

Prenatal diagnosis of glycogenosis type II was performed by direct assay of acid alpha-glucosidase (EC 3.2.1.20) in chorionic villous biopsy obtained by transcervical cannula aspiration from a pregnancy at risk in the 10th week of gestation. The exact value of the enzyme activity estimated by the use of antibody preparations for purified human liver acid alpha-glucosidase was in the heterozygous range, and so the homozygous enzyme deficiency could be excluded. The subsequent analysis of cells cultured from amniocentesis sampling in the 18th week of gestation resulted in a similar outcome. The study with antibodies showed that in 23 control chorionic villi obtained during gestational ages between 7-13 weeks, 1-15% of the total alpha-glucosidase activity at pH 4.0 were due to renal or neutral enzyme. This indicates that it may be important to employ antibodies for prenatal diagnosis using chorionic villous sampling. A healthy and unaffected boy was born. The biochemical values obtained from an umbilical blood specimen were in accordance with the results of the prenatal diagnosis.

Adult↗
PubMed1985

Diagnosis of Pompe's disease using leukocyte preparations. Kinetic and immunological studies of 1,4-alpha-glucosidase in human fetal and adult tissues and cultured cells.

Kinetic and immunological studies of 1,4-alpha-glucosidase show that the distribution of acid, renal and neutral alpha-glucosidase at pH 4.0 and 6.5 is as follows: in liver and cultured fibroblasts and amniotic fluid cells the activity at pH 4.0 is mainly due to the acid enzyme. Even at pH 6.5, the activity is largely due to the residual activity of the acid enzyme. In kidney and leukocytes, however, the activity by acid enzyme at pH 4.0 represents only 30-60% of the total activity and the remaining activity is from renal enzyme. At pH 6.5, the activity is almost exclusively of renal enzyme. Renal alpha-glucosidase has a higher affinity for maltose (Km, 0.8 mmol/l) than acid enzyme, however; for glycogen acid enzyme shows the highest affinity (20.7 g/l). There is no significant difference in the kinetic characteristics of alpha-glucosidase between fetal and adult tissues. In kidney, however, a relative increase in renal enzyme to acid enzyme with age is found, i.e. in fetal kidney the alpha-glucosidase activity at pH 4.0 is more than twice that at pH 6.5, whereas in adult kidney, the activity ratio at pH 4.0-6.5 is approximately 1. Antibodies for human liver acid alpha-glucosidase decrease the alpha-glucosidase activity in normal leukocytes by 22-75% at pH 4.0 (0.54-3.8 nmol/min per mg protein). The decrease is significantly lower in patients with Pompe's disease (0-0.11 nmol/min per mg protein) as well as in their parents and some siblings (0.15-0.70).

Adult↗
PubMed1984

Glycosylated haemoglobin and glycosylated albumin: evaluation of different methods in diabetic control.

The levels of glycosylated haemoglobins and albumin were determined in 56 diabetic patients aged between 5 and 19 years. The glycohaemoglobin levels were measured by two different methods, cation-exchange chromatography and a colorimetric chemical method. The glycosylated albumin levels were measured by a chemical method in plasma albumin purified with Affi-gel Blue. The results were compared with other indicators such as blood glucose and urinary glucose. The postprandial blood glucose levels were well correlated with the levels of glycoproteins: glycohaemoglobin by the column method (r = 0.886), glycohaemoglobin by the chemical method (r = 0.72) and glycoalbumin (r = 0.662). The urinary levels of glucose showed a weak correlation with blood glucose levels (r = 0.214) and with glycoalbumin (r = 0.298), but no correlation with glycohaemoglobin. Significant correlations between the changes of glycosylated albumin levels and glycohaemoglobin were found (r = 0.78). The result of the comparison of the chemical method with the column method for glycohaemoglobin determination showed a high correlation between the values (r = 0.95). There were significant differences in glycosylated protein levels between normal and diabetics. There were also significant differences in glycohaemoglobin and glycoalbumin values between fairly managed and poorly managed groups of diabetics. Of the three parameters, glycoalbumin, glycohaemoglobin and plasma glucose, the greatest absolute changes were found in the levels of glycoalbumin.

Adolescent↗
PubMed1983

Prenatal diagnosis of galactosemia and properties of galactose-1-phosphate uridyltransferase in erythrocytes of galactosemic variants as well as in human fetal and adult organs.

The kinetic characteristics and isoelectrofocusing patterns of uridyltransferase and the concentrations of galactose-1-phosphate in hemolysates were investigated in a family with compound variants of Duarte and classical galactosemia. There were no significant differences in Km values between the genotypes. However, the isoelectrofocusing study with thin-layer polyacrylamide gels (PAGIF) as well as with agarose gels (AGIF) showed a distinctive difference. The enzyme from the Duarte variant resolved into at least two more activity bands at pH between 5.2 and 5.4. The accumulation of galactose-1-phosphate was observed only in homozygotes for classical galactosemia. Compound heterozygotes (G-D) without any clinical manifestations did not show an accumulation of galactose-1-phosphate. The isoelectrofocusing study of the enzyme in human tissues revealed their activity resolving into multiple bands, 6-8 bands at pH 5.50-6.00 and 1-3 bands at pH 4.9-5.2. No significant differences were found in the patterns between fetal and adult liver except that the intensity of the anodic bands (pH 4.9-5.2) was weaker in fetal tissues. Prenatal diagnosis of classical galactosemia was performed in nine families by measuring the enzyme activity in cultivated amniotic fluid cells. Absence of the enzyme activity in amniotic fluid cells was found in two cases, and in four cases the heterozygosity was diagnosed by a relative low enzyme activity, 30-50% of the activity in control cells cultured in parallel.

Amniotic Fluid↗
PubMed1983

Fatal lipid storage myopathy with deficiency of cytochrome-c-oxidase and carnitine. A contribution to the combined cytochemical-finestructural identification of cytochrome-c-oxidase in longterm frozen muscle.

Two newborn female siblings fell ill with apathy, failure of suckling and a generalized progressive muscular hypotonia. Death occured at the age of 7 weeks, obviously caused by impairment of respiratory musculature. Biochemical studies in one child revealed carnitine deficiency especially in skeletal muscle; hepatic encephalopathy was absent. Both children had a generalized hyperaminoaciduria, an unusual finding in primary carnitine deficiency. Besides fatty metamorphosis of the liver, bilateral hydroureters and tubular calcifications of both kidneys, morphological studies showed a generalized lipid storage myopathy which predominated in Type-I-fibres and was accentuated in the muscles of the neck. Enzymehistochemical electron microscopy in longterm frozen muscle demonstrated that cytochrome-c-oxidase activity was absent not only in myopathic but also in most of the morphological unchanged muscle fibres. Only some fibres and endothelial cells displayed normal activity of mitochondria. Biochemically no cytochrome aa3 (cytochrome-c-oxidase) could be found in skeletal muscle; cytochrome b was almost undetectable. --In newborns with fatal lipid storage myopathy and carnitine deficiency it seems necessary to look for additional defects in the respiratory chain. Enzyme histochemical electron microscopy is a sensitive method in identifying cytochrome-c-oxidase even after a 12 months period of storage.

Carnitine↗
PubMed1983

A radioisotopic method for fructose-1-phosphate aldolase assay that facilitates diagnosis of hereditary fructose intolerance.

A sensitive new method in which D-[U-14C]fructose-1-phosphate is used for fructose-bisphosphate aldolase (EC 2.1.2.13) assay is described. The radioactive fructose-1-phosphate compound was prepared from [U-14C]fructose by use of partly purified fructokinase (EC 2.7.1.4). With this method we measured normal values for aldolase in human liver (2.4-10.0 nmol/min per mg of protein), kidney (3.6-3.8), and intestine (4.2-10.0) as well as Km values for fructose-1-phosphate (approximately 1.0-2.2 mmol/L). In patients with hereditary fructose intolerance the aldolase activity in liver and intestine was less than 10% of normal values. The Lineweaver-Burk plots for data from patients with hereditary fructose intolerance were hyperbolic, indicating a structural alteration in the enzyme.

Adult↗