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Biomedical subjects

Z Deyl

Publications and source records attributed to Z Deyl.

At least 109 records · Page 6Linked to original sources
PubMed1981

Changes in pyridinoline content of elastin during ontogeny.

It has been shown that, contrary to desmosine and isodesmosine, the content of pyridinoline increases in elastin preparations obtained from rat and bovine aortae and from bovine ligmentum nuchae throughout the whole lifespan. The molar proportion of this cross-linking amino acid is within the range of 0.6 - 2.5 leucine equivalents per 100 amino acid residues.

Aging↗
PubMed1981

Discrimination analysis as a tool for classifying the value of biochemical and immunological tests in lung cancer.

The data obtained with routine biochemical, immunological and haematological tests in healthy blood donors and in patients with lung cancer were subjected to discrimination analysis with the aim to select the minimum possible combination of methods with the highest probability of distinguishing between the two groups. Transformation of lymphocytes (TR.LY) after PHA stimulation, formation of E-rosettes (E-ROS), and blood glycoproteins (GP) were shown to permit the most complete differentiation between the group of patients and the blood donors. On the basis of the above-mentioned tests the discrimination rule could be defined: IF 52,73249 - 0.45913 X E-ROS - 0.40752 X TR.LY + 0.02790 X GP greater than or equal to 0, then the investigated person is classified as a cancer patient while at values less than 0 the person is classified as a healthy individual.

Computers↗
PubMed1981

High fat diet induced fluorescence and increased resistance of collagen to proteolytic cleavage.

Feeding of animals with high fat diets results in a distinct increase in the stability of the collagen structure as reflected by its higher resistance towards proteolytic cleavage. It appears that covalent cross links are formed when the experimental animals are fed a diet containing a high proportion of unsaturated fatty acids, i.e. when the chance of the formation of reactive intermediates is increased. This is based on the observation of the presence of non-reducible high molecular weight collagenous material in pepsin treated collagen. This high molecular weight fraction exhibited a typical 390/460 nm fluorescence and a distinct decrease of lysine content. It is suggested that the observed phenomena result from the action of in vivo present potential cross-linking agents.

Animals↗
PubMed1981

The effect of food restriction and low protein diet upon collagen type I and III ratio in rat skin.

It has been demonstrated that the content of the collagen type I is more affected by both chronic low protein diet feeding and chronic food deprivation (50% food intake) than the content of collagen type III. By introducing these dietary regimes the proportion of collagen type I to collagen type III ratio drops from 2.1 to 1.3 indicating the higher proportion of collagen type III in the skin at the end of the experiment (after 18 months of chronic feeding). It was also observed that the total concentration of hydroxyproline (hyp) in the skin decreases considerably in both food restricted animals and those fed a low protein diet. It is suggested that, under the present experimental conditions, the balance between collagen break-down and synthesis is shifted and, furthermore, that this shift is different for collagen type I and III and results in an altered ratio of these two collagen species in the skin. Refeeding of animals leads to a higher than normal collagen type I to III ratio indicating thus a relatively higher proportion of collagen type I in this tissue.

Animals↗
PubMed1980

Studies on the chemical nature of elastin fluorescence.

Two fluorescent fractions were found in total acid hydrolysate of elastin. The fraction with higher chromatography mobility in isopropyl alcohol/conc. ammonia/water (9 : 1 : 2) was purified by multiple preparative paper chromatography in the same solvent system, and by gel chromatography on Sephadex G-25, ion-exchange chromatography on phosphocellulose and another gel chromatography on Sephadex G-10. The purified material was chromatographically homogeneous, had an ultraviolet absorption maximum at 315 nm and exhibited a strong 320/405 nm fluorescence. 1H- and 13C-NMR spectra were in good agreement with those published previously [6] for pyridinoline, a lysine derived fluorescent compound in collagen. The major part of the fluorescent material present in acid hydrolysate of elastin was always contaminated, even after complex purification procedures. It is concluded that elastin contains several fluorophores, one of which is a cross-linking tricarboxylic amino acid with a pyridinium ring having very probably the structure of 3-(2-amino-2-carboxyethyl)-1-(5-amino-5-carboxy-2-hydroxy-pentyl)-4-(3-amino-3- carboxypropyl)-5-hydroxypyridinium. The position of 2-amino-2-carboxyethyl and 3-amino-3-carboxypropyl residues has not been definitely established and can be interchanged.

Amino Acids↗
PubMed1980

Two-dimensional thin-layer chromatography of Dns-amino acids on reversed-phase silica gel.

Ready-for-use reversed-phase high-performance thin-layer chromatographic plates were used for the separation of Dns-amino acids. The development was performed by using methanol-2% acetic acid (75.25) or methanol-0.01 M Na2HPO4 (75:25). Reversed-phase plates were used also for adsorption chromatography using a non-aqueous solvent system such as benzene-chloroform-acetic acid (50:48:2) or n-heptane-ethyl acetate-acetic acid (65:33:2). Good separations were achieved by using both principles in the two-dimensional arrangement.

Acetates↗
PubMed1980

Effect of cartilage bone marrow extract on the metabolism of collagen in osteoarthrotic cartilage.

The effect of cartilage bone marrow extract (CBME) on the metabolism of collagen and proteoglycan in crude embryo and human cartilage was investigated. While in chick embryos' articular cartilages the increased levels of radioactivity in collagen and proteoglycan were observed, in normal human cartilage only slight changes were detected. In osteoarthrotic cartilages, however, a marked increase in radioactivity was found in collagen and in the proteoglycan fraction containing the glycoprotein link. A blockade of collagenolysis by CBME treatment is suggested.

Animals↗
PubMed1980

gamma-Carboxyglutamic acid-containing protein of rat kidney cortex. Changes with high fat diet, and molecular parameters.

It was shown that the level of gamma-carboxyglutamic acid-containing protein is increased in perfused rat kidney after long-term administration (60 and 350 days) of a high-fat diet. No difference was found between the effect of vegetable fat and animal fat. Concomitantly it was shown that the relative molecular weight, N-terminal sequence over four residues, the profile of chymotryptic peptides and the sequence around the two (of the three in total) gamma-carboxyglutamic acid residues (over the span of seven residues) are identical with those found previously in osteocalcin and the gamma-carboxyglutamic acid-containing protein isolated from at least partially calcified connective tissue.

1-Carboxyglutamic Acid↗
PubMed1980

Evaluation of biochemical and immunological parameters in patients with lung cancer by discrimination analysis.

Data obtained by biochemical and immunological tests in a group of healthy blood donors and a group of patients with lung cancer were subjected to discrimination analysis in order to find the minimum possible combination of methods which permit reliable differentiation of the two groups., It was revealed that the lymphocyte transformation after stimulation with PHA, the formation of E rosettes and the plasma level of glycoproteins permit complete differentiation between the group of patients and healthy controls. Based on the above three tests discrimination rules can be defined. If 52.73249--0.45913.ROS--0.40752. TRLY + 0.02790 GP greater than or equal to 0, the investigated subject can be included in the group of patients, when the values are smaller, the subject is healthy.

Alpha-Globulins↗
PubMed1980

Contribution to the mode of action of glycosaminoglycan-polysulphate (GAGPS) upon human osteoarthrotic cartilage. Biochemical study of the collagen and proteoglycan turnover.

The effect of glycosaminoglycan polysulphate (GAGPS) upon the metabolism of proteoglycan (PG) and collagen in chick embryos and human cartilage was studied. GAGPS treatment caused an accumulation of studied compounds. According to the results with osteoarthrotic cartilages the marked increase of radioactivity in collagen and PG (mainly in the fraction containing glycoprotein link) is due to the inhibition of catabolic processes.

Animals↗