PubMed Health⌕ Search

Biomedical subjects

K Osterlund

Publications and source records attributed to K Osterlund.

At least 37 records · Page 2Linked to original sources
PubMed1983

Causes of neonatal deaths in a pediatric hospital neonatal unit. An autopsy study of a ten-year period.

A study is presented of 1020 consecutive autopsies on newborn infants who died during the first 28 days of life at the Children's Hospital, University of Helsinki, during 1969-1978. The infants were grouped into four categories according to their weight at birth and into early (0-7 days) and late (8-28 days) neonatal groups according to their age at death. 77.5% of the cases fell into the early neonatal group. The most common causes of death were hyaline membrane disease (HMD) and cerebral haemorrhage (CH), which together accounted for 41.9% of all the deaths. Congenital anomaly was the second most common group of causes, comprising 35.3% of the cases. A gradual fall in the total number of deaths was conspicuous during the ten-year period. There was a statistically significant decrease in the number of deaths from HMD and CH in the weight categories 1001-1500 g and 1501-2500 g. The fall is considered to reflect improvement in both obstetrics and neonatal medicine.

Autopsy↗
PubMed1982

Essential charged amino acids in the binding of fibronectin to gelatin.

The binding of fibronectin to gelatin-agarose was strictly dependent on pH, having a pH optimum of 7-9. The binding was strongly inhibited by increasing ionic strength. A chemical modification of lysyl and arginyl groups of fibronectin abolished the binding activity. The anionic detergents sodium dodecyl sulphate and sodium deoxycholate in concentrations of 10-100mM had the same effect. The binding was not affected by the non-ionic detergents Triton X-100, Tween 20 or Lubrol WX. The results demonstrate an important role of ionic interactions in the binding of fibronectin to gelatin. Absence of inhibition by non-ionic detergents suggests that hydrophobic interactions contribute relatively little to the binding of fibronectin to gelatin.

Amino Acids↗
PubMed1981

Treatment of maternal hyperthyroidism with antithyroid agents and changes in thyrotrophin and thyroxine in the newborn.

Eleven pregnant women with concomitant hyperthyroidism were treated with antithyroid drugs. At monthly intervals serum thyroxine (T4) and triiodothyronine (T3) were measured with radioimmunoassay, the Sephadex uptake of radioactive triiodothyronine (T3U) determined the free T4 and T3 indices calculated (FT4I, FT3I). TSH-binding inhibiting immunoglobulins (TBII) were determined by the radiomembrane assay. Serum TSH and T4 were measured at delivery from cord blood and/or from the newborn infants some days after birth. Serum TSH was significantly elevated in one infant. There was an inadequate post-partal rise in serum T4 concentration in this child and in another who showed only a marginal elevation of TSH. The mothers of these infants were given carbimazole in doses of 30 and 25 mg/day, respectively, at the time of delivery. No significant changes were seen in other infants, the daily doses being 20 mg of carbimazole or less. There was no clinical indication of hypo- or hyperthyroidism in any of the newborn. The TBII were positive in most patients and there was a trend of normalization during treatment. No relationship between the dose of antithyroid drug and the level of TBII could be seen. During treatment the dose was adjusted according to the FT3I values. This seems to be an adequate laboratory test for this purpose.

Adult↗
PubMed1980

Resonance Raman spectra of Pseudomonas cytochrome c peroxidase.

Resonance Raman spectra of ferric, ferrous and ferrous-carbonyl forms of Pseudomonas cytochrome c peroxidase are presented. The porphyrin ring vibration frequencies are compared with those of other heme proteins which are in well defined spin and oxidation states. Both the native oxidized and the reduced forms of the enzyme show two sets of Raman lines, one having a low-spin and the other a high-spin character. Resolved bands can be assigned to heme c and heme c', the low-spin and the high-spin moiety of the enzyme, respectively. The low-spin heme moiety of the ferric enzyme is concluded to have an imidazole-nitrogen : heme-iron : methionine-sulphur hemochrome structure, whereas in the ferrous enzyme the methionine-sulphur ligation is exchanged with the nitrogen of histidine or lysine (N epsilon). The Raman spectra indicate that the high-spin ferric heme consists of a mixture of a five-coordinated form and a six-coordinated form with a carboxylate group as a ligand. In the reduced enzyme the high-spin heme is five-coordinated. The Raman spectrum of the carbonyl derivative of Pseudomonas cytochrome c peroxidase indicates that the compound has an electron structure similar to that of carboxyhemoglobin and carboxymyoglobin. The data confirm earlier results that the two heme moieties of the enzyme are bound to the apoprotein by covalent thioether bonds as in c-type cytochromes.

Carbon Monoxide↗
PubMed1980

Ultrastructure of the cell wall of a Synechocystis strain.

The ultrastructure of the cell wall of a Synechocystis strain, isolated from the Gulf of Finland, was studied using several electron microscopic techniques. This cyanobacterium has numerous projections which were observed to penetrate the cell wall complex. An additional layer (AL) was associated with the outer membrane. An additional external wall layer (EL) was connected to the outer membrane complex by thin fibers as revealed by ruthenium red staining. A hexagonal arrangement of the subunits in the additional external wall layer with a lattice constant of 15.5 nm was found.

Cell Wall↗
PubMed1979

Resonance Raman study on yeast cytochrome c peroxidase. Effect of coordination and axial ligands.

Resonance Raman spectra are reported for native ferric cytochrome c peroxidase, its cyanide and fluoride compounds, those of the ferrous enzyme and its cyanide and carbonyl compounds, and the spectrum of the hydrogen peroxide compound, compound I. Band frequencies of ferric horseradish peroxidase isoenzyme C2 and its derivatives are also given. Comparison of the frequencies of the bands around 1400, 1500, 1560-1580, and 1610-1640 cm-1 with those of other hemoproteins and heme model compounds showed that in ferric highspin compounds in particular the bands are not only spin and oxidation sensitive, as has previously been reported, but that they also reflect the coordination of the heme iron. It is suggested that ferric cytochrome c peroxidase and horseradish peroxidase are pentacoordinated. In the hexacoordinated fluoride, cyanide and carbon monoxide derivatives the bands reflect the spin state and the out-of-plane position of the heme iron. The spectrum of cytochrome c peroxidase compound I supports previous studies that suggest that it has a lowspin heme iron in the Fe(IV) oxidation state.

Binding Sites↗
PubMed1971

[Rooming-in].

Explore the source record for details and available documents.

Female↗