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Biomedical subjects

M Potier

Publications and source records attributed to M Potier.

At least 145 records · Page 8Linked to original sources
PubMed1983

Urinary alpha-L-fucosidase in cystic fibrosis.

The binding of the urinary lysosomal enzyme alpha-L-fucosidase to free- and Sepharose 4B-bound concanavalin A has been compared in cystic fibrosis (CF) patients and normal controls. The concentration of methyl-alpha-D-mannoside necessary to prevent 50% of total alpha-L-fucosidase activity to bind to free and bound concanavalin A (Ki, 50%) was similar for CF (0.68 +/- 0.20 and 1.3 +/- 0.3 mmol/l, respectively) and normal controls (0.53 +/- 0.18 and 1.9 +/- 0.5 mmol/l, respectively). The CF and normal urinary alpha-L-fucosidase also showed similar pH optima (4.8), Km, app (0.071 and 0.074 mmol/l, respectively) and thermodenaturation curves at 44 degrees C (t1/2 = 108 min). We report that the kinetic and the concanavalin A-binding affinity of alpha-L-fucosidase are similar from urine of cystic fibrosis patients and controls.

Concanavalin A↗
PubMed1982

Characterization of human placental neuraminidases. Stability, substrate specificity and molecular weight.

1. At least two components of neuraminidase can be distinguished on the basis of thermolability and sedimentability by using the artificial fluorogenic substrate 4-methylumbelliferyl N-acetyl-alpha-D-neuraminate. 2. In crude homogenates, thermodenaturation at 25 degrees C showed a biphasic curve corresponding to component A (half-life, 21 min) and B (half-life, 85 min). The two components were partially resolved by centrifugation. A being soluble and B sedimentable. Both had similar pH-activity curves (pH optimum, 4.4), Km values (A, 0.10 mM; B, 0.06 mM) and molecular weight as determined by radiation inactivation (A, 67000; B, 63000). 3. The soluble A form was still aggregated or bound to membranous debris since almost all neuraminidase activity was eluted near or at the void volume of a Sephacryl S-300 column. 4. Both soluble and sedimentable fractions of placenta hydrolysed the GD1A ganglioside and N-acetyl-neuraminyl-D-lactose linearly for 12 h but no fetuin hydrolysis was detected. 5. The neuraminidase activity with the artificial fluorogenic substrate was inhibited by N-acetylneuraminyl-D-lactose but not by the GD1A ganglioside. These preliminary results suggest that there exist two closely related enzymes hydrolysing both the artificial substrate and N-acetylneuraminyl-D-lactose and a third one hydrolysing the GD1A ganglioside exclusively.

Chromatography, Gel↗
PubMed1982

Separation of amniotic fluid cell types in primary culture by Percoll density gradient centrifugation.

Amniotic fluid cells obtained by transabdominal amniocentesis at 15-17 weeks of gestation and cultured for 15 and 21 days were separated into three fractions by density gradient centrifugation in Percoll. Each fraction (or peak) corresponded to the following densities: peak A, 1.02-1.03 g/ml; peak B, 1.04-1.05; peak C, 1.05-1.06. Peak A was composed of both non-viable and viable cells; the latter adopted the morphology of epithelial cells in culture. Peak B contained a mixture of fibroblasts and epithelioid cells and peak C had only epithelioid cells. The variability of N-acetyl-beta-hexosaminidase and alkaline phosphatase activities was reduced in peaks B and C as compared to that of peak A and of unseparated cells suggesting that more defined and homogeneous cell types for enzymatic determinations can be obtained by centrifugation in Percoll density gradient. In prenatal diagnosis of biochemical defects, the separation of cells would permit a more precise diagnosis by eliminating enzyme variability due to the presence of different cell types or non-viable cells.

Acetylglucosaminidase↗
PubMed1982

Maternal alphafetoprotein screening by the polypropylene tube immunoradiometric assay on dried blood.

The polypropylene tube immunoradiometric assay for alphafetoprotein (AFP) determination was applied to maternal serum along with a radioimmunoassay technique during the second trimester of pregnancy. Blood from pregnant women was collected by finger prick on strips of chromatography paper (Schleicher and Schuell No. 903C) and air dried. A 4.75 mm disc spot was eluted in anti-AFP coated tubes containing 1.0 ml of assay medium. After one hour the medium was vortexed and the tubes washed and counted on a Concept 4tm (Micromedic Systems, Horsham, PA. 19044). The sensitivity of the technique is about 9 micrograms/l (35 ng/l in the assay) by the Rodbard formula. The concordance between the dried blood and the serum RIA tests in normal pregnancies was over 90 per cent at the 95th and 97th percentiles. This assay on dried blood spotted on chromatography paper was tested on 1003 patients and proved to be an ideal alternative to whole serum screening techniques: it minimizes sample manipulations and can easily be integrated into an existing newborn screening programme.

Female↗
PubMed1982

Oral lecithin and linoleic acid in Friedreich's ataxia: I. Design of the study, material and methods.

A clinical and biochemical evaluation of twenty-two patients with Friedreich's Ataxia and ten normal controls was undertaken in 1980 to assess the effect of lecithin and linoleic acid supplements on the course of the disease. The trial consisted of two consecutive six months periods on either supplements in a double-blind crossover fashion. Clinical appraisal was performed with regards to the following parameters: joints mobility, muscle strength, equilibrium, coordination, motor accuracy, speech and numerous day to day activities. Blood samples were obtained at the beginning and in the course of the trial for enzymatic determinations. This paper describes the methodology of the study.

Administration, Oral↗
PubMed1982

Oral lecithin and linoleic acid in Friedreich's ataxia: II. Clinical results.

Twenty-two patients with Friedreich's Ataxia and ten normal controls were followed for one year and assessed as to their clinical performance after two successive six-month periods of lecithin or safflower oil. Results demonstrated no significant difference in performance scores according to group assignation, neither in patients nor in controls. According to stages, two patients in stage I and to a lesser degree, one patient in stage IV showed better scores for muscle strength and some motor accuracy and coordination tests with lecithin. Controls as groups maintained positive scores in all tests. Patients as groups showed negative mean values in nine out of eleven tests. Again as groups, patients receiving safflower oil demonstrated a mean 8% less deterioration than patients receiving lecithin. This study demonstrates that objective clinical tests and the participation of normal controls are a must in a therapeutic trial implicating patients with a progressive disorder such as Friedreich's Ataxia. The possible role of linoleic acid as the active factor from which clinical improvement proceeded in some specific patients and with early functional stages of the disease, has to be considered and reevaluated in the near future.

Administration, Oral↗
PubMed1982

Oral lecithin and linoleic acid in Friedreich's ataxia: III. Biochemical results.

Lecithin and safflower oil brought about the same changes in serum LAD activity and kinetics in patients with Friedreich's Ataxia as in controls when results of this double-blind crossover study were analyzed according to group assignation. According to functional stages, pretrial LAD activity decreased with advancing severity while Km for lipoamide increased. Lecithin and safflower oil supplements corrected the elevated Km for lipoamide but produced a further reduction in LAD activity. These changes may have been due to the increased intake of linoleic acid, a precursor of lipoic acid, which is present in high percentage in both lecithin and safflower oil. Results of the biochemical study thus agreed with the clinical data gathered during the course of the one-year trial in suggesting that linoleic acid may well have been the active factor through which biochemical and clinical improvement was previously observed in patients with Friedreich's Ataxia supplemented with lecithin.

Administration, Oral↗
PubMed1981

Gene for neuraminidase activity on mouse chromosome 17 near h-2: pleiotropic effects on multiple hydrolases.

The low activity of liver neuraminidase that is characteristic of mouse strain SM/J is inherited as a single gene on chromosome 17, near the major histocompatibility complex. This gene, neuraminidase-1 (Neu-1), is represented by the low activity allele Neu-1s in SM/J and the high activity allele Neu-1b in C57BL/6J and most other strains. Previously described variations in the posttranslational processing of acid phosphatase, alpha-mannosidase, arylsulfatase-B, and alpha-glucosidase are attributed to pleiotropic effects of this gene.

Alleles↗
PubMed1981

beta-Galactosidase-neuraminidase deficiency in adults: deficiency of a freeze-labile neuraminidase in leukocytes and fibroblasts.

4-methylumbelliferyl neuraminidase activity was studied in fibroblasts, leukocytes, and frozen tissues from adult patients with beta-galactosidase-neuraminidase deficiency and specific clinical manifestations. This enzyme was almost completely deficient in fibroblasts, but the residual activity was relatively high (20% of the control mean) in the leukocytes from the patients. The frozen liver from one patient showed the enzyme activity as high as controls. This enzyme consisted of two components, freeze-labile and freeze-stable, and it was demonstrated that only the labile enzyme was deficient in fibroblasts and leukocytes. The apparently normal activity of neuraminidase in frozen autopsy tissues of a patient may be explained by the loss of the labile component in control tissues after a long-term freezing. The neuraminidase activity was variable in parents and no definite conclusion was drawn on the hereditary nature of the disease.

Brain↗
PubMed1981

Development of proteolytic activity in rabbit fetal intestine.

The development of proteolytic activity was determined in rabbit fetal intestine using 125I-hemoglobin as substrate. This assay method allowed increased sensitivity and complete linearity with incubation time and amount of homogenate protein. The effect of pH on substrate hydrolysis showed two main peaks of activity around pH 5 and 8. The apparent Km of proteolytic activity for the 125I-hemoglobin substrate was 0.57 mg/ml at pH 8. Proteolytic activity increases about 10-fold in fetal rabbit intestine between 21 and 31 days of gestation.

Animals↗
PubMed1981

Control of disaccharidase activities in brush-border membranes of guinea pig fetuses: a role of pancreatic proteases?

The intestinal brush-border disaccharidases most resistant to pancreatic protease digestion in vitro are lactase and trehalase. When compared to maltase and sucrase, they are also those which showed the largest increase during development of guinea pig fetuses. These results suggest that pancreatic proteases may play a role in the control of brush-border disaccharidase activities during fetal development.

Animals↗
PubMed1980

Studies on the sialidoses: properties of human leucocyte neuraminidases.

At least two components of neuraminidase (acylneuraminyl hydrolase, EC 3.2.1.18) can be distinguished in human leucocytes on the basis of pH optimum, thermolability at 30 degrees C and the effect of the detergent octyl-beta-D-glucoside. With 4-methylumbelliferyl-alpha-D-N-acetylneuraminate as substrate, the A component has a pH optimum of 5.0, is labile at 30 degrees C and is unaffected by 0.2 M octyl-beta-glucoside. The B component has a pH optimum of 4.0-4.2, is stable at 30 degrees C but loses most of its activity in the presence of 0.2 M octyl-beta-glucoside. Both A and B components are membrane-bound but only the A component is solubilized by octyl-beta-glucoside in an active form. Molecular weights of neuraminidases by gamma-ray radiation inactivation (a method that does not require solubilization of the enzyme) were found to be 240 000 +/- 19 000 for the B component, 203 000 +/- 17 000 for the A component and 238 000 +/- 8000 for the octyl-beta-glucoside-solubilized A component. Gel filtration of soluble A component on Sephacryl S-300, in the presence of octyl-beta-glucoside, showed a single peak of activity eluted at or near the void volume suggesting that the enzyme is still in an aggregated form. Profound deficiency of neuraminidase activity was found for both A and B components in leucocytes of patients affected with sialidoses type 1 and 2 (less than 15% normal) and intermediate activity in obligate heterozygotes. These results suggest that the A and B components of leucocyte neuraminidase are closely related from the genetic point of view and that rapid diagnosis of sialidoses can be done by fluorimetric assay of neuraminidase in leucocytes.

Adolescent↗