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Biomedical subjects

M Sarnecka-Keller

Publications and source records attributed to M Sarnecka-Keller.

At least 19 recordsLinked to original sources
PubMed1984

Sugar constituents of the seromucoid in insulin-dependent diabetes.

Seromucoid glycoproteins reveal different carbohydrate composition in diabetic patients as compared with normal subjects. An increased glucose content is the most characteristic feature of seromucoid found in diabetic patients. The amounts of proteins, neutral sugars, amino-sugars and sialic acids in seromucoid correlate with diabetic microangiopathy.

Adult↗
PubMed1984

Osmotic resistance of rat erythrocytes in hyperinsulinism and streptozotocin-diabetes as compared with cholesterol and sialic acid contents of erythrocyte ghosts.

The osmotic resistances of rat erythrocytes compared with the contents of some ghost constituents were studied in rats with normal insulin level, insulin deficiency (streptozotocin diabetes) and in hyperinsulinism. In streptozotocin-diabetes rat erythrocytes a higher than control resistance to osmotic haemolysis was found. This was accompanied by and increased volume of erythrocytes, a lower yield of ghost isolation, higher cholesterol and lower than normal sialic acid contents. Insulin treatment of rats induced a lowered osmotic resistance of erythrocytes. This was connected with an increase in erythrocyte volume and yield of ghost isolation. Simultaneously a decrease in membrane cholesterol content of sialic acids were observed.

Animals↗
PubMed1983

Free and protein-bound rat serum peptides.

Some of the free serum peptides circulate in blood bound to the serum proteins. Conditions used in protein precipitation influence the peptide affinity to the protein. The lability of the bonds between peptides and their carrier proteins may be of physiological importance.

Animals↗
PubMed1983

Glycine and serine rich peptides isolated from rat liver preparations enriched with smooth endoplasmic membranes.

Three electrochromatographic homogeneous peptides belonging to acidic, basic and neutral electrophoretic glycopeptide fractions isolated from rat liver preparations enriched with smooth endoplasmic membranes contain a very high level of glycine and serine and only a slight level of phenylalanine but do not contain tyrosine. Their amino acid compositions differ chiefly in the contents of basic and acidic amino acids.

Animals↗
PubMed1981

Comparison of rat plasma glycoprotein composition with biochemical activity and morphology of liver Golgi apparatus in streptozotocin diabetes treated with insulin.

The seromucoid level and its neutral sugar composition were studied and the results compared with Golgi-enriched membrane UDP-Gal leads to GlcNAc transferase activity and the morphology of the liver Golgi apparatus in situ. Four groups of rats were studied: 1. control, 2. streptozotocin diabetic, 3. insulin treated, and 4. streptozotocin diabetic and insulin treated. In many respects a correlation was observed between the seromucoid level and composition and the biochemical and morphological properties and composition and the biochemical morphological properties of the Golgi apparatus.

Animals↗
PubMed1980

Morphology of the Golgi apparatus in streptozotocin-diabetic rat liver.

The altered morphology of the Golgi apparatus in streptozotocin-diabetic rat liver is described in situ and in preparations of the Golgi-membrane-enriched fraction. The main differences, as compared with controls, are a diminished Golgi apparatus area, the rounding of stacks of cisternae and the absence of secretory vacuoles with VLDL granules. These findings are discussed in view of biochemical alterations found previously in the Golgi-membrane-enriched fraction isolated from streptozotocin-diabetic rat liver.

Animals↗
PubMed1980

Influence of middle-molecular-weight solutes from dialysate on the migration rate of leukocytes.

To investigate further the biologic activity of solutes in the middle-molecular-weight range, we studied the influence of these compounds on the migration of unseparated white blood cells and separated granulocytes and lymphocytes. Middle molecules (MM) inhibit the migration of unseparated leukocytes, but this effect on lymphocytes was seldom observed. With scanning electron microscopy, unseparated leukocytes were shown to adhere to one another, forming cellular clumps. This phenomenon could not be seen when separated cells were used. These results give some insight into the mechanism of inhibition exerted by MM and into the changes, observed in earlier experiments, of cellular composition of skin exudate obtained from untreated patients with uremia.

Cell Aggregation↗
PubMed1979

Th activities of perfused livers of control and streptozotocin diabetic rats in the synthesis of some plasma proteins and peptides.

By measuring the incorporation of 14C-DL-leucine a decreased capacity of isolated perfused steptozotocin diabetic rat liver to synthetize plasma total proteins, albumin and the seromucoid fraction was found as compared with a control. The relative rate of synthesis of the seromucoid proteins calculated as proportional to the rate of synthesis of albumin or the total plasma proteins was approximately twice as great as in control liver. 14C-DL-leucine was also incorporated in perfused liver into the nonprotein but non-dialysable sugar-peptide fraction but the synthesis of the glycopeptide components of this fraction was markedly reduced in diabetic rat liver.

Animals↗
PubMed1978

Middle-sized ninhydrin-positive molecules in uraemic patients treated by repeated haemodialysis. II. Chief peptide constituents of the faction.

The fraction of middle-sized molecules obtained from haemodialysate by chromatography on Dowex 50W x 8 resolves upon thin-layer electrophoresis on Sephadex G-25 into nine ninhydrin-positive fractions and one staining only with tolidine reagent. All ten electrophoretic fractions give similar filtration profiles with Bio-Gel P-6 in the presence of SDS and 2-mercaptoethanol. The chief peptide components common to each electrophoretic fraction have molecular weight approx. 3000 and are especially abundant in lysine, glycine, glutamine acid and serine, while aromatic amino acids are in very low concentration.

Amino Acids↗
PubMed1978

Biochemical activity and morphology of the Golgi apparatus in alloxan diabetic rats.

In Golgi-enriched membrane fraction isolated from alloxan diabetic rat liver, the protein content is lower but the protein composition is similar to normal. The specific activity of galactosyl transferase in this membrane fraction is higher than normal, but the total activity of the enzyme in the whole liver is normal. Great dispersion is found among the individual values. Differences in the specific activities of some other marker enzymes were also found in the Golgi-enriched membrane fraction. The morphology of the Golgi complex examined in either thin sections of Golgi-enriched fraction or ultra-thin sections of livers appears normal. A slight reduction of the rough endoplasmic reticulum is observed. The results obtained are discussed in comparison with those obtained for streptozotocin diabetic rat liver.

Animals↗