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1.
Tijdschr Psychiatr ; 61(3): 188-193, 2019.
Article in Dutch | MEDLINE | ID: mdl-30896030

ABSTRACT

BACKGROUND: Mindfulness based stress reduction (mbsr) has been demonstrated to result in a reduction of stress and improvement of well-being in both healthy volunteers and the general population.
AIM: To examine the effect of mbsr on burnout symptoms, well-being and professional development in medical, surgical and psychiatric residents. METHODS A randomised controlled trial of 148 medical, surgical and psychiatric residents of the Radboud umc, half of whom immediately participated in mbsr and half after a three-month waiting period. Self-report questionnaires were administered online before and after the intervention and waiting list period. Effect of mbsr on professional development was explored with a qualitative interview with a purposive sample of 19 residents six months after completion. RESULTS No differences were found between the mindfulness and waitlist group regarding emotional exhaustion in the study population as a whole. However, those with high level of burnout symptoms benefitted significantly more from the course than the others. In addition, participants in the mindfulness group demonstrated a higher competence, less worry and more mindfulness skills, self-compassion and empathy. In terms of professional development, residents reported improvements in self-awareness, insight, acceptance, resilience and relating to others.
CONCLUSION: mbsr could result in a reduction of symptoms for medical and surgical residents with a high level of burnout symptoms. For the medical and surgical residents as a whole, mindfulness may enhance their professional development in several areas.


Subject(s)
Burnout, Professional/prevention & control , Mindfulness , Stress, Psychological/prevention & control , Students, Medical/psychology , Adult , Empathy , Female , Humans , Internship and Residency , Male , Mindfulness/methods , Waiting Lists
2.
Science ; 279(5357): 1710-1, 1998 Mar 13.
Article in English | MEDLINE | ID: mdl-9497287

ABSTRACT

Process improvements in silica membrane fabrication, especially the use of clean-room techniques, resulted in silica membranes without detectable mesoscopic defects, resulting in significantly improved transport properties. Supported membranes calcined at 400 degreesC were 30 nanometers in thickness, showed a H2 permeance at 200 degreesC of 2 x 10(-6) moles per square meter per second per Pascal (mol m-2 s-1 Pa-1), and had a CH4 permeance more than 500 times smaller. Molecules larger than CH4 were completely blocked. Silica membranes calcined at 600 degreesC showed no detectable CH4 flux, with a H2 permeance of 5 x 10(-7) (mol m-2 s-1 Pa-1) at 200 degreesC. These results signify an important step toward the industrial application of these membranes such as purification of H2 and natural gas as well as the selective removal of CO2.

4.
Ann Clin Biochem ; 28 ( Pt 2): 179-82, 1991 Mar.
Article in English | MEDLINE | ID: mdl-1859157

ABSTRACT

We describe a modification of the second-derivative spectrophotometric assay for carboxyhaemoglobin in blood. Using the original procedure we have often observed a time-dependent change in the signal leading to unreliable results. By using phosphate-buffered-saline (pH 7.4) instead of ammonia to dissolve the deoxygenating agent (sodium dithionite), we obtained stable and reproducible second-derivative signals from which the percentage carboxyhaemoglobin in the patients' samples can be calculated.


Subject(s)
Blood Chemical Analysis , Carboxyhemoglobin/analysis , Spectrophotometry , Evaluation Studies as Topic , Humans
6.
Phys Rev Lett ; 62(2): 221-224, 1989 Jan 09.
Article in English | MEDLINE | ID: mdl-10039954
9.
J Chromatogr ; 378(2): 283-92, 1986 Jun 13.
Article in English | MEDLINE | ID: mdl-3733988

ABSTRACT

A newly devised procedure for a simultaneous determination of urinary tetrahydroaldosterone and aldosterone is described. The procedure is based on deconjugation and acetalization, followed by extraction and derivatization of the urinary compounds to their trimethylsilyl ethers and subsequent gas chromatographic-mass fragmentographic detection. To evaluate the assay, aliquots of a urine sample of a healthy individual were analysed in multiplicate; a mean tetrahydroaldosterone concentration of 103 nmol/l and a within-sample, within-day- and day-to-day coefficient of variation of 1.8, 3.2 and 3.4%, respectively, were found. Determination of aldosterone in the same sample yielded a mean concentration of 25.3 nmol/l and the following coefficients of variation: 2.8% (within-sample), 3.8% (within-day) and 4.3% (day-to-day). The urinary excretion of tetrahydroaldosterone and aldosterone in 24-h urine portions was determined in twenty healthy individuals, aged 23-77 years; for tetrahydroaldosterone and aldosterone, an excretion of 94 +/- 66 nmol per 24 h and of 40 +/- 22 nmol per 24 h was found, respectively, in accord with the literature. An example of the usefulness of the described assay is given by establishing the cause of severe salt-wasting in an infant; a highly elevated tetrahydroaldosterone and aldosterone excretion was demonstrated, proving that the child suffered from unresponsiveness to aldosterone (pseudohypoaldosteronism).


Subject(s)
Aldosterone/analogs & derivatives , Aldosterone/urine , Adult , Aged , Female , Gas Chromatography-Mass Spectrometry , Humans , Infant , Male , Middle Aged
12.
Biochim Biophys Acta ; 701(2): 180-4, 1982 Feb 18.
Article in English | MEDLINE | ID: mdl-7041979

ABSTRACT

Treatment of spectrin, insulin, glucagon and ribonuclease with ozone results in covalent cross-linking of these proteins. This cross-linking is not reversed by treatment with dithiothreitol and thus can not be ascribed to -S-S- bond formation. A concomitant O,O'-dityrosine formation is observed by spectrofluorometric analysis of the protein and by amino acid analysis and thin-layer chromatography of hydrolyzed protein samples. It is highly probable that the observed protein cross-linking should be attributed to interpeptide O,O'-dityrosine bonds. Several authors have shown before that oxidation of proteins with horseradish peroxidase and H2O2 also leads to O,O'-dityrosine formation. Peroxidase-induced O,O'-dityrosine formation in galactose oxidase (d-galactose:oxygen 6-oxidoreductase, EC 1.1.3.9) causes a strong increase of enzyme activity. In accordance with these observations ozone treatment of galactose oxidase also leads to O,O'-dityrosine formation with a concomitant 8-fold increase of enzyme activity.


Subject(s)
Ozone/pharmacology , Proteins , Tyrosine/analogs & derivatives , Amino Acids/analysis , Cross-Linking Reagents/pharmacology , Galactose Oxidase/metabolism , Glucagon/analysis , Humans , Insulin/analysis , Macromolecular Substances , Proteins/analysis , Ribonucleases/analysis , Spectrin/analysis , Spectrometry, Fluorescence , Tyrosine/analysis
13.
Biochim Biophys Acta ; 647(1): 87-94, 1981 Sep 21.
Article in English | MEDLINE | ID: mdl-7295723

ABSTRACT

Exposure of spectrin to visible light in the presence of a photosensitizer results in photo-oxidation of sensitive amino acid residues and covalent cross-linking of the polypeptides. In a previous paper the cross-linking was ascribed to a secondary reaction between photo-oxidized histidine residues and amino groups. The following observations, described in this paper, are in accordance with this supposition. (1) During illumination of spectrin in the presence of a photosensitizer a pronounced photo-oxidation of histidine residues takes place. (2) Simultaneously a decrease of free amino groups is observed. (3) Semicarbazide protects against cross-linking and is bound to a histidine photo-oxidation product in spectrin. (4) The pH profile of histidine photo-oxidation and subsequent reaction with amino groups is similar to the pH profile of spectrin cross-linking. Amidination of NH2 groups in spectrin does not inhibit cross-linking, as visualized by gel electrophoresis. On the other hand aminidation of denatured myoglobin causes a 50% inhibition of cross-linking. These observations support the notion of NH2-involvement in cross-linking but also demonstrate, that other photodynamic cross-link mechanisms exist.


Subject(s)
Membrane Proteins/metabolism , Spectrin/metabolism , Amino Acids/metabolism , Cross-Linking Reagents , Electrophoresis, Polyacrylamide Gel , Erythrocyte Membrane/metabolism , Glycine/metabolism , Humans , Myoglobin/metabolism , Photochemistry , Protoporphyrins/metabolism , Semicarbazides/metabolism
15.
Biochim Biophys Acta ; 602(3): 591-9, 1980 Nov 18.
Article in English | MEDLINE | ID: mdl-7437422

ABSTRACT

Semicarbazide can interfere with oxidative processes in the red blood cell membrane via different modes of action. Treatment of human red blood cell membranes with O3, results, among other effects, in cross-linking of membrane proteins and inhibition of glyceraldehyde-3-phosphate dehydrogenase activity. Semicarbazide inhibits these effects by acting as an O3 scavenger. The effect of semicarbazide as an O3 scavenger is complicated by the fact that ozonolysis of semicarbazide yields a product that causes inhibition of glyceraldehyde-3-phosphate dehydrogenase. Glyceraldehyde-3-phosphate dehydrogenase inhibition can also be provoked by incubation of membrane suspensions with O3-treated phospholipids. Semicarbazide prevented this effect by interaction with an inhibitory O3-phospholipid reaction product. Protoporphyrin-induced photodynamic cross-linking of membrane proteins is chemically distinct from O3-induced cross-linking. Photodynamic cross-linking is also inhibited by semicarbazide, in this case via reaction with a histidine photooxidation product.


Subject(s)
Erythrocyte Membrane/drug effects , Erythrocytes/drug effects , Ozone/blood , Semicarbazides/pharmacology , Erythrocyte Membrane/metabolism , Glyceraldehyde-3-Phosphate Dehydrogenases/blood , Humans , In Vitro Techniques , Membrane Proteins/blood , Models, Chemical , Ozone/pharmacology , Phospholipids/pharmacology , Photochemistry
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