Biomedical subjects

P Hintz

Publications and source records attributed to P Hintz.

5 recordsLinked to original sources

PubMed1990

[Quantifying aortic valve insufficiency using color Doppler echocardiography].

UNLABELLED: 51 consecutive patients with the clinical signs of aortic valve incompetence (AI) were evaluated by color-coded Doppler flow mapping (CDF) before angiography (AG). Quantitation of the severity of AI was performed by measurement of length and width of the extension of regurgitant jet (grade I-IV). After AG results both -AG and CDF- were compared. In 36 patients the results of both methods concurred exactly by use length in CDF. With CDF, the regurgitation was overestimated in 7 cases by one grade and underestimated in 8 patients also by one grade. Width of regurgitant jet relative to size of outflow space is a useful parameter to distinguish between mild and severe A1 (limit 0.50). CONCLUSION: CDF is a suitable method for semiquantitative assessment of AI. In presence of unequivocal CDF signs and in consideration of clinical and other patients findings AG will be dispensable before aortic valve replacement.

Adolescent↗

PubMed1987

Neutral proteinase inhibitors in PMN leukocytes. I. Purification and characterization of a neutral proteinase inhibitor from bovine neutrophils.

An inhibitor of neutral proteinases was isolated from the cytosol of bovine leukocytes by anion exchange chromatography on Mono Q and gel filtration on a HPLC TSK column. The gel filtration resulted in two fractions with inhibitory activity which could be identified by sodium dodecyl sulphate-poly-acrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions as dimer and monomer of the inhibitor. The latter was shown to be homogeneous in SDS-PAGE with an apparent molecular mass of 40 kDa, with calibrated HPLC a molecular mass of 36.5 kDa has been determined. Isoelectric focusing followed by Western blot analysis revealed four bands in the pH range of 5.0 to 5.9. The inhibitor was found in bovine polymorphonuclear neutrophils (PMN), whereas lymphocytes and monocytes lacked this protein. No immunological cross-reactivity between the described cell-derived PMN-inhibitor (PMN-I) and alpha 1-proteinase inhibitor was detectable. The mechanism of inhibition for the serine proteinases chymotrypsin, trypsin, pancreatic elastase and leukocyte elastase was studied. PMN-I could not bind to PMS-chymotrypsin. The reaction of the serine proteinases with the PMN-I was characterized by the determination of the association rate constant kon.

Animals↗

PubMed1986

Metal ion-induced activation of molecular oxygen in pigmented polymers.

Diamagnetic and paramagnetic metal ions enhanced the rate of production of hydrogen peroxide during autoxidation of melanin pigments, as measured using an oxidase electrode. However, redox-active metal ions, such as Fe3+ and Cu2+, caused a marked decrease in H2O2 production. Evidence for redox-active metal ion-dependent formation of hydroxyl radicals during autoxidation of melanin pigments has been obtained using the electron spin resonance-spin trapping method. Evidence for direct reduction of Fe3+ by melanin polymers also has been obtained using optical spectroscopy. Mechanisms of molecular activation of oxygen induced by metal ions on melanin polymers are discussed.

Animals↗

PubMed1986

An electron spin resonance study of free radicals from catechol estrogens.

Electron spin resonance spectroscopy has been used to demonstrate production of semiquinone free radicals from the oxidation of the catechol estrogens 2- and 4-hydroxyestradiol and 2,6- and 4,6-dihydroxyestradiol. Radicals were generated by horseradish peroxidase/H2O2 or tyrosinase/O2, or by autoxidation, and were detected as their complexes with spin-stabilizing metal ions (Zn2+ and/or Mg2+). Radical production occurs via one- or two-electron oxidation of catechol estrogens, depending on the type of activating system. Autoxidation of catechol estrogens produces superoxide and H2O2 at physiological pH values. The present results also indicate a difference in the reactivity of quinones derived from 2- and 4-hydroxyestradiol. The toxicological significance of these reactions is discussed.

Animals↗

PubMed1985

Mechanism of dismutation of superoxide produced during autoxidation of melanin pigments.

The hydrogen peroxide produced during the autoxidation of melanin pigments has been measured using an oxidase electrode. The autoxidation has been shown to occur via the superoxide intermediate. The melanin pigment competes with superoxide dismutase for the scavenging of superoxide radicals. However, superoxide dismutase at high concentrations caused a substantial increase in the production of hydrogen peroxide, formed during melanin autoxidation. The implications of this finding are discussed in light of melanin's ability to function as a pseudo-dismutase.

Animals↗