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Biomedical subjects

H Braun

Publications and source records attributed to H Braun.

At least 91 records · Page 5Linked to original sources
PubMed1983

Statistical models for evaluation of pleural effusions.

Statistical models designed to aid in the identification of neoplastic effusions were formulated. A computer program utilizing n-chotomous, multivariate probit analysis was used for estimation of model parameters. These parameters were estimated for an illustrative sample of 88 patients with effusions of unknown etiology. The outstanding feature of the statistical approach is its potential as a diagnostic and research tool. Regarding its diagnostic potential, if carcino-embryonic antigen (CEA) levels of plasma (PLAS-CEA) and pleural fluid (PLFL-CEA) were used separately, PLAS-CEA values greater than 4.833 ng/ml and PLFL-CEA values greater than 4.193 ng/ml discriminated malignant from benign effusions. Elevated CEA levels in conjunction with cell block examination noticeably improved diagnostic efficacy. The thresholds are consistent with CEA levels found by other investigators. Furthermore, the method employed is specific in predicting the probability that a given effusion is malignant. Regarding its research potential, the efficacy of different sets of tests in predicting malignancy can be simultaneously and comparatively evaluated.

Adult↗
PubMed1982

Lead encephalopathy treated by versenate (CA-EDTA).

A patient with generalised epileptic seizures, mental and psychotic signs was diagnosed as suffering from lead encephalopathy. He was a big consumer of home-made arrack, illicit alcohol prepared at home in secrecy, in tools containing copper and lead. Basophilic stippling increased the possibility of lead encephalopathy, which was soon proved. He was successfully treated with low doses of Versenate, a chelating factor, and totally recovered.

Chelating Agents↗
PubMed1982

[The cell number in spontaneous uncentrifuged urine].

The leucocytes and erythrocytes in spontaneous urines were determined in the counting chamber at native and experimentally reduced pH values after standing for various periods. The pH value remained constant for up 6 h, whereby the disintegration of cells increases with rising pH values. The investigations do not rule out a circadian rhythm of cell excretion referring to the quantity of cells/time. Depending on the absolute number of cells the methodic variation coefficient lies between 4 and 25%.

Adult↗
PubMed1981

Does postural asymmetry indicate directionally of rotation in rats: role of sex and handling.

Postural asymmetry of male and female Wistar rats was assessed during 4 tests: (a) tail suspension, (b) tail holding, (c) tail pinch and (d) walking on a narrow path. The tests were conducted prior to and after (+)-amphetamine (1 mg/kg, i.p.) administration. Rotational directionality was assessed in a rotometer. Only in female rats did postural adjustment during the tail-pinch predict with borderline significance the direction of circling prior to and after amphetamine. In both surgically castrated and conjugated estrogen-treated male rats, in sham-castrated and handled males, the tail-pinch test caused the same dominant directionality as rotation under amphetamine. The duplicity of postural tests suggests that there is a multitude of systems controlling and modulating postural response.

Animals↗
PubMed1980

Postural asymmetry and directionality of rotation in rats.

The hypothesis [12] that the direction of postural asymmetry can predict rotational side preferences caused by amphetamine, was tested. Postural asymmetry of male and female Wistar rats was assessed using four tests: (a) tail suspension, (b) tail holding, (c) tail pinch, and (d) walking on a narrow path. The tests were conducted prior to and after (+)-amphetamine (1 mg/kg, IP) administration. Rotational directionality was assessed in a rotometer. None of the tests predicted the direction of circling. The findings suggest that there is a multitude of systems contributing to asymmetric posture.

Animals↗
PubMed1980

A 3 1/2-year experience with double-lumen implants in breast surgery.

The use of the double-lumen implant, with 20 mg of Solu-Medrol or less, has improved the final results in patients having reconstruction after mastectomy. However, the results in patients having augmentation mammaplasties have been much more dramatic, with far superior results over those patients having a gel implant. During the first year the incidence of scar tissue problems is 17 times greater with the gel implants than with the double-lumen implants and 20 mg or less of Solu-Medrol. Scar capsules were also extremely amenable to closed capsulotomy after augmentation with the double-lumen implant, in marked contrast to the gel implant. There is no evidence to support the hypothesis that the double-lumen implant and Solu-Medrol merely delays the eventual appearance of the scar tissue problem. The recommended dosage of Solu-Medrol would appear to be 20 mg and not less.

Breast↗
PubMed1979

Carcinogenicity of di(N-nitroso)-perhydropyrimidine (DNPP) after intraperitoneal application to rats.

Male Sprague-Dawley rats received 30 mg/kg body wt. (group I) or 15 mg/kg (group II) di(N-nitroso)-perhydropyrimidine (DNPP) by the intraperitoneal route once a week for life. The DNPP treatment significantly reduced the life expectancy in both groups. DNPP induced tumors of the esophagus (27% incidence in group I, 33% in group II) and possibly also of the liver (4% incidence in group I, 8% in group II).

Animals↗
PubMed1977

External yeast beta-fructosidase: stereospecific labeling by [3H]conduritol-beta-epoxide and isolation of labeled peptides from the active site.

1. External yeast beta-fructosidase (beta-D-fructofuranoside fructohydrolase EC 3.2.1.26) was labeled by [3H]conduritol-B-epoxide, an active-site directed inhibitor of this enzyme. During the inactivation 1--2 mol of inhibitor were bound covalently per mol of enzyme. The labeled enzyme was digested with pepsin and 3H-labeled peptides were isolated. 2. Conduritol-B-epoxide is a racemic mixture of 1-D-1,2-anhydro-myo-inositol and 1-L-1,2-anhydro-myo-inositol, but only the latter one was now shown to be the reactive component. 3. The label was released from the enzyme by milk alkaline treatment and identified by paper chromatography as 1-D- or L-chiro-inositol, which suggested that an ester linkage had been formed by reaction of the epoxide with a carboxylate group at the active site of the enzyme. Position and role of this carboxylate group are discussed.

Affinity Labels↗
PubMed1977

Differential scanning calorimetry of the thermal denaturation of lactate dehydrogenase.

1. Differential scanning calorimetry has been used to study the thermal denaturation of lactate dehydrogenase. At pH 7.0 in 0.1 M potassium phosphate buffer, only one transition was observed. Both the enthalpy of denaturation and the melting temperature are linear function of heating rate. The enthalpy is 430 kcal/mol and the melting temperature 61 degrees C at 0 degrees C/min heating rate. The ratio of the calorimetric heat to the effective enthalpy indicated that the denaturation is highly cooperative. Subunit association does not appear to significantly contribute to the enthalpy of denaturation. 2. Both cofactor and sucrose addition stabilized the protein against thermal denaturation. Pyruvate addition produced no changes. Only a small time-dependent destabilization was observed at low concentrations of urea. Large effects were observed in concentrated NaCl solutions and with sulfhydryl-modified lactate dehydrogenase.

Animals↗
PubMed1977

Stereospecific ring opening of conduritol-B-epoxide by an active site asparatate residue of sucrase-isomaltase.

Conduritol-B-epoxide inactivates sucrase-isomaltase (sucrose alpha-glucohydrolase, EC 3.2.1.48-dextrin 6-alpha-glucohydrolase, EC 3.2.1.10) irreversibly with incorporation of 1 mol inhibitor/mol subunit, the affinity label being bound in both subunits to a beta-carboxyl group of an aspartic acid (Quaroni, A. and Semnza; G. (1976) J. Biol. Chem. 251, 3250-3253). Conduritol-B-epoxide is a racemic mixture of 1-L-1,2-anhydro-myo-inositol and 1-D-1,2-anhydro-myo-inositol, but only the latter one is the reactive component, since 1-L-1,2-anhydro-myo-inositol alone did not inactivate the enzyme. After inactivation by 1-D-1,2-anhydro-myo-inositol the label was released by hydroxylamine and identified as scyllo-inositol. One can decide now which C atom of the epoxide ring has been attacked by the enzyme's aspartate residue. This explains why only the D-enantiomer is the reactive species and provides further information about the role of the carboxylate residue during enzymic hydrolysis.

Animals↗