Search PubMed⌕ Search

Biomedical subjects

E Egger

Publications and source records attributed to E Egger.

At least 145 records · Page 8Linked to original sources
PubMed1981

Temperature dependent rise in activity of horseradish peroxidase caused by non-ionic detergents and its use in enzyme-immunoassay.

Non-ionic detergents such as polyoxyethylene-octylphenol or -sorbitolester were found to increase activity of horseradish peroxidase due to delay of inactivation in the course of substrate reaction. This rise in activity was investigated using different chromogens and was highest with o-dianisidine. An increasing stability of the enzyme to higher reaction temperatures was observed when detergents were added to the substrate solution, and the action of detergents also is enhanced with increasing reaction temperature and time. Different degrees of activation were found when comparing substrate conversion with and without detergents using free peroxidase (2.7-fold) and conjugated peroxidase bound to the solid phase by antigen antibody reaction (1.8-fold). In enzyme-immunoassay, detection limit and analytical sensitivity can be doubled.

Antigen-Antibody Reactions↗
PubMed1980

[CT and lymphography correlations in the evaluation of patients with testicular tumours (author's transl)].

27 patients with testicular tumours were examined by lymphography and computerized tomography for evaluation of metastatic spread in the retroperitoneal lymphnodes. A good correlation of results was found in 23 patients. In 4 cases lymphography failed to show metastatic disease, which was easily recognized by CT. In account of the lymphatic spread pathways of testicular tumours leading mainly to the lymphnodes close to the kidney pedicle CT appears to be method of choice in the staging of these patients, as the lymphnodes in this area are often not demonstrated by lymphography. Computerized tomography allows the exact localisation and extension of neoplastic lymphnodes and at the same time a good evaluation of the surrounding organs.

Dysgerminoma↗
PubMed1979

Suitability of commercial control sera for the quality control of activity determination of alkaline phosphatase.

The suitability of thirteen commercially available control sera for measuring alkaline phosphatase (EC 3.1.3.1; orthophosphoric acid monoester phosphohydrolase, ALP) activity in human serum was tested. Apart from differences in ALP activity observed in some reconstituted commercial sera, the behaviour of control materials towards experimental variables such as the nature and concentration of the substrate, pH and type of buffer (or PO4-acceptor) together with the composition of the isoenzymes present in human serum highlights the problems and difficulties if commercial materials are to be used as control sera. The half-saturation constants in control sera were in all cases smaller than those of ALP isoenzymes from bone and liver. The shape of substrate activity curves and the pH optimum in most of control sera differed from that of human serum. The discrepant kinetic data of control materials and human serum may mask or suggest changes relevant to commercial quality control serum but not to samples of human serum.

Alkaline Phosphatase↗
PubMed1979

Creatine kinase isoenzyme BB in serum of healthy adults and children.

The activity of the creatine kinase isoenzyme BB was determined in the serum of 26 healthy adults and 31 children. The isoenzyme BB could be proved as a normal component in the human serum. In the adults examined, an activity of 0.56 +/- 0.16 I.U./l (x +/- S.D.) was determined. The activity of creatine kinase isoenzyme BB in the serum does not depend on sex but is subject, however, to a strong age dependence. Only at an age of more than 18 years, isoenzyme BB activities adjust to those of adults.

Adult↗
PubMed1979

Stability of isoenzymes of alkaline phosphatase in various buffer systems.

The stability of isoenzymes of alkaline phosphatase from liver, bones and small intestine was compared after addition to inactivated serum in the buffer systems: glycine, 2-amino-2-methyl-1-propanol, diethanolamine and 2-amino-2-methyl-1,3-propandiol at 37 degrees C. The mentioned isoenzymes were inactivated to different extents in glycine and 2-amino-2-methyl-1-propanol buffers. In diethanolamine and 2-amino-2-methyl-1,3-propandiol buffers sufficient stability of isoenzymes is obtained so that only these buffers are suitable for activity determinations of alkaline phosphatase at 37 degrees C.

Alkaline Phosphatase↗
PubMed1978

The apoenzyme of aspartate aminotransferase and alanine aminotransferase in the serum of healthy persons and patients suffering from liver diseases.

In activity determination with addition of pyridoxal 5'-phosphate (P-5-P), aspartate aminotransferase (AST) activity increases by 6.5 U/l and that of alanine aminotransferase (ALT) by 2.5 U/l in the serum of healthy persons. This corresponds to a relative stimulation of initial activity by 37% and 15.2%, respectively. ApoAST activity in patients with chronic liver diseases is not changed as compared with that of healthy persons, the relative stimulation rate, however, is significantly smaller. ApoALT activity and corresponding relative stimulation is significantly greater as compared with healthy persons. In the case of acute viral hepatitis, a decrease of AST and ALT activity is followed by a decrease of apoenzyme activity in the course of disease. Diagnostic evidence of determinations of aminotransferase activities could not be improved by addition of P-5-P.

Alanine Transaminase↗