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Biomedical subjects

K Mortensen

Publications and source records attributed to K Mortensen.

At least 37 records · Page 2Linked to original sources
PubMed1998

Retinal detachment after cataract extraction in myopic eyes.

PURPOSE: To determine the incidence of retinal detachment (RD) after cataract extraction in people 40 years of age or older with axial myopia (i.e., axial length > or = 25.5 mm). SETTING: Fifteen Danish eye clinics. METHODS: Two hundred forty-five eyes had cataract extraction performed at 15 eye clinics; 237 eyes had extracapsular cataract extraction (ECCE) and 8 eyes, intracapsular cataract extraction (ICCE). Postoperative data were reported by the practicing ophthalmologists. Mean follow-up was 27 months (range 14 to 32 months). RESULTS: Five RDs occurred in the 245 eyes (2.0%). Excluding the ICCE cases and the two cases of combined cornea transplantation and ECCE, RD occurred in 4 of the 235 eyes that had ECCE (1.7%). The incidence after ECCE with posterior chamber lens implantation was 1.4%. Complete postoperative status was reported on 158 eyes. Forty-eight eyes (30.4%) had a neodymium:YAG capsulotomy and 3 (6.0%) developed an RD 1, 3.5, and 21 months after the capsulotomy. CONCLUSION: The RD incidence after ECCE with posterior chamber lens implantation was low but higher than that in unselected populations. The incidence increased after laser capsulotomy.

Adult↗
PubMed1998

The epidemiology of hospital-referred head injury in northern Norway.

This retrospective population-based survey describes the epidemiology of head injury in a defined population in Northern Norway. It includes all 247 patients with head injury referred to the University Hospital of Tromsø, Norway, during 1993. Head injury was defined as physical damage to the brain or skull caused by external force. The annual incidence rate of hospital-referred head injury was 229/100,000 population with a male preponderance of 1.7:1.0. The cause was a fall in 62%, road traffic accident in 21% and assault in 7% of the cases. The observed incidence rate is low despite the use of wide inclusion criteria, probably due to a decrease in road traffic accidents. A further decrease in the number of head injuries in our region may be achieved by preventing falls.

Accidental Falls↗
PubMed1997

Nucleotide cofactor-dependent structural change of Xenopus laevis Rad51 protein filament detected by small-angle neutron scattering measurements in solution.

Rad51 protein, a eukaryotic homologue of RecA protein, forms a filamentous complex with DNA and catalyzes homologous recombination. We have analyzed the structure of Xenopus Rad51 protein (XRad51.1) in solution by small-angle neutron scattering (SANS). The measurements showed that XRad51.1 forms a helical filament independently of DNA. The sizes of the cross-sectional and helical pitch of the filament could be determined, respectively, from a Guinier plot and the position of the subsidiary maximum of SANS data. We observed that the helical structure is modified by nucleotide binding as in the case of RecA. Upon ATP binding under high-salt conditions (600 mM NaCl), the helical pitch of XRad51.1 filament was increased from 8 to 10 nm and the cross-sectional diameter decreased from 7 to 6 nm. The pitch sizes of XRad51.1 are similar to, though slightly larger than, those of RecA filament under corresponding conditions. A similar helical pitch size was observed by electron microscopy for budding yeast Rad51 [Ogawa, T., et al. (1993) Science 259, 1896-1899]. In contrast to the RecA filament, the structure of XRad51.1 filament with ADP is not significantly different from that with ATP. Thus, the hydrolysis of ATP to ADP does not modify the helical filament of XRad51.1. Together with our recent observation that ADP does not weaken the XRad51.1/DNA interaction, the effect of ATP hydrolysis on XRad51.1 nucleofilament should be very different from that on RecA.

Adenine Nucleotides↗
PubMed1997

Structure and thermodynamics of nonideal solutions of colloidal particles: investigation of salt-free solutions of human serum albumin by using small-angle neutron scattering and Monte Carlo simulation.

The understanding of the structural and thermodynamic properties of moderately or highly concentrated solutions is fundamental, e.g., in medicine and biology and also in many technical processes. In this work, we have used the small-angle neutron scattering method (SANS), in combination with Monte Carlo simulation, to study salt-free solutions of human serum albumin (HSA) in the concentration range up to 0.26 g ml-1. The model calculations of the theoretical SANS intensities are quite general, thus avoiding the approximation that the relative positions and orientations of the particles are independent of each other. The computation of the theoretical intensities also includes the calculation of a "thermodynamic' intensity scattered at zero angle, which is obtained via the nonideal part of the chemical potential. The latter quantity is obtained by applying the test particle method during the Monte Carlo simulations. It is found that the SANS data can be explained by a model where the HSA molecules behave as hard ellipsoids of revolution with semiaxes a = 6.8 nm, b = c = 1.9 nm. In addition to the hard core interaction, the particles are also surrounded by a soft, repulsive rectangular-shaped potential which is spherically oriented around the particles. The combination of SANS and statistical thermodynamics also allows a determination of the nonideal part of the chemical potential and the activity coefficient of HSA. As expected the activity coefficient deviates strongly from the value one (several powers of ten) already at fairly low concentrations: the effects are comparable to, or even larger than, for instance hydrophobic or van der Waals interaction.

Chemical Phenomena↗
PubMed1995

Evidence for elongation of the helical pitch of the RecA filament upon ATP and ADP binding using small-angle neutron scattering.

Structural changes of the RecA filament upon binding of cofactors have been investigated by small-angle neutron scattering. Both ATP and ADP increased the helical pitch of the RecA homopolymer, which is observed to be 7 nm in the absence of any cofactor. The binding of ATP altered the pitch to 9 nm, whereas the binding of ADP only produced a pitch of 8.2 nm. The pitch determined for the RecA complex with the ATP analog adenosine 5'-[gamma-thio]triphosphate was similar to that found with ATP. Thus, at least three, somewhat different. RecA helical filamentous structures may form in solution. The binding of DNA to RecA did not alter the pitch significantly, indicating that the cofactor binding is the determining factor for the size of the helical pitch of the RecA filament. We also found that elongation of the helical pitch is a necessary, but not a sufficient condition, for the coprotease activity of RecA. The presence of acetate or glutamate ions is also required. The pitch of the ADP.RecA filament is in agreement with that found in the crystal structure. This correlation indicates that this structure corresponds to that of the ADP.RecA filament in solution, although this is not the species active in recombination.

Adenosine Diphosphate↗
PubMed1994

Small-angle scattering study of alpha 1 inhibitor III from rat blood plasma.

The alpha 1 proteinase inhibitor III from rat blood plasma, homologous to the alpha 2-macroglobulin family of proteins, has been studied in solution using small-angle scattering of X-rays and of neutrons: the radius of gyration, Rg, was found to be 4.5 nm, and the largest distance within the molecule, Dmax = 14 nm. When the inhibitor reacts with chymotrypsin or methylamine, the resulting derivatives yield slightly higher Rg-values, 4.7 and 4.85 nm, respectively. The data of the native protein are consistent with a model, the projection of which resembles the letter V and which is formed by the two identical halves of an elliptic cylinder with semi-axes of 2.1 and 5.5 nm and a length of 11 nm. This elliptic cylinder model also explained the scattering from the monomeric complement proteins C3 and C4, as well as that from the monomers of the dimeric and tetrameric alpha 2-macroglobulin family of proteins (Osterberg, R., et al. (1991), Biochemistry 30, 7873-7878). Due to the conformational change occurring when the thiol ester bond is split, the cleft in the V-form seems to be closed; and as a result, the models of the chymotrypsin and methylamine derivatives are more compact than that of the native protein.

Acute-Phase Proteins↗