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Biomedical subjects

O Schmut

Publications and source records attributed to O Schmut.

At least 73 records · Page 4Linked to original sources
PubMed1976

[The attack of different proteases on isolated zonular fibers (author's transl)].

Some proteases, i.e. trypsin, alpha-chymotrypsin, thermolysin, proteinase K, alpha-amylase, collagenase, and papain were investigated on their effect on isolated zonular fibers. All these enzymes but collagenase were zonulolytic active. An attack on the ground substance of the fibers by substances solving glycosaminoglycans and proteoglycans (hyaluronidase, EDTA, guanidinium chloride, H2O2) showed an increased effect of the enzymes used. These results suggest that the interfibrillar matrix has a protective function on the zonular fibers.

Amylases↗
PubMed1976

[Quantitative determination of antiproteinases in human tears (author's transl)].

By quantitative determination of antiproteinases, i.e. alpha1-antitrypsin, alpha1-antichymotrypsin, and inter-alpha-trypsin inhibitor normal values could be obtained. The importance of antiproteinases is demonstrated in this paper. Especially alpha1-antitrypsin was very easy to quantitate and might be of diagnostic interest.

Chymotrypsin↗
PubMed1976

[Conformational changes of hyaluronic acid in acid medium (author's transl)].

Both vitreous body homogenate and a fibrous product containing hyaluronic acid and collagen isolated from vitreous humor by acetone precipitation were investigated to elucidate the liquefaction of vitreous body by acids. Graphic evaluation of the titration with hydrochlorid acid and viscosity measurements suggest a changed of the hyaluronic acid molecule in the pH-range between 5.2 and 4.1. Between these pH-values the ionization of carboxyl groups is decreased accompanied by conformational changes of the hyaluronic acid molecule. These results are in agreement with the conclusion of other authors that by lowering the pH of hyaluronic acid solutions a random coil to double helix transition of hyaluronic acid occurs.

Animals↗
PubMed1975

Studies on the generation of hydrogen peroxide during some non-enzymic reactions changing the hyaluronic acid molecule.

The effect of catalase on non-enzymic-induced changes in the conformation of hyaluronic acid in a vitreous humour preparation was measured using viscometry. Ascorbate, heavy metal ions, riboflavin or EDTA all lowered the viscosity of hyaluronic acid solutions. These effects could be prevented by the addition of catalase. This suggested that H2 O2 is produced by these compounds and that the resulting change in conformation of hyaluronic acid may be due to peroxyl and hydroxyl attack by the free radicals thus generated.

Animals↗
PubMed1975

[Qualitative and quantitative determination of prealbumin, retinol-binding protein, Gc-globulin and C4-component in aqueous humor (author's transl)].

By using the combined disc-immunomethod, prealbumin, retinol-binding protein Gc-globulin, and C4-component were identified in human aqueous humor. These proteins can be quantitatively analyzed by single radial immuno-diffusion. The quantiative determination of retinol-binding protein and C4-component in aqueous humor could be of diagnostic value because retinol-binding protein is capable of transporting retinol (vitamin A), and C4-component is implicated in immunologic reactions. Moreover, it is noteworthy that by these immunologic methods it is possible to determine protein concentrations below 0.05 mg/100 ml.

Aqueous Humor↗
PubMed1975

[Quantitative determination of aqueous humor proteins by electroimmodiffusion in an antiserum containing agarosegel (author's transl)].

An exact quantitation of aqueous humor proteins within a few hours can be attained by an modification of the quantitative estimation of the proteins by electrophoresis in agarose gel established by Laurell. The aqueous humor proteins form long immunoprecipitations in agargel. The length of the precipitats is proportional to the concentration. By determination of albumin, coeruloplasmin and transferrin the application can be pointed out.

Albumins↗
PubMed1975

[Electron microscopic investigations of vitreous collagen after treating the vitreous with liquefying substances (author's transl)].

By electron microscopic studies collagenase, hyaluronidase, HCl, ascorbic acid, and iron ions have been found to attack the collagen fibers of bovine vitreous. Because of the possible role of ascorbic acid in collagen synthesis and the ability of ascorbic acid to degrade hyaluronic acid and collagen we suggest that the ascorbic acid of the vitreous essentially participates in construction and metabolism of the vitreous body.

Animals↗
PubMed1975

[The proof of different types of collagen in the bovine eye (author's transl)].

Characteristically stained polyacrylamide gels can be obtained by disk-electrophoresis in acid medium of several tissues of the bovine eye. The technique permits to prove different types of collagen in the eye, and allows the differentiation and identification of the tissues. By these results the different tissues of the eye can be divided into three groups. 1. Tissues showing two alpha collagen components in polyacrylamide gel (cornea, sclera, iris, ciliary body, anterior lens capsule, and the pigmented epithelium of the retina). 2. Tissues possessing one alpha component only (zonula fiber and vitreous body). 3. Tissues which show neither the alpha nor the beta and gamma component of collagen (lens nucleous and retina without pigmented epithelium).

Animals↗
PubMed1975

[The influence of riboflavin on vitreous homogenate (author's transl)].

Sunlight causes a decrease of viscosity of a mixture of riboflavin and ox vitreous homogenate while without riboflavin no reaction can be observed. The mechanism of this reaction is not yet clarified. It is possible that the reaction is closely related with the degradation of the viscosity of a hyaluronic acid solution by ascorbic acid cause of the production of H2O2 in both reactions. As an other mechanism the transfer of light energy on hyaluronic acid by riboflavin can be assumed.

Animals↗