Biomedical subjects
Publications and source records attributed to U Weber.
Till now few reported cases of alveolar soft part sarcoma of the skeletal musculature which was classified for the first time by Christopherson in 1952 could not make plain a uniforme treatment. Radioresistance was also described as unsuccessful chemotherapy as early or excessiv surgical proceeding. Our own unusual observation of a case of this very rare malignant mesenchymal tumor may give a direction for a sensible therapy.
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Osseous ruptues of the ulnar collateral ligament in the metacarpophalangeal joint of the thumb are to be found more frequently in experimental ruptures at an isolated preparation than they are described in clinical examinations. It must positively be achieved to re-affix also a small avulsion fragment to do not remove the entire compound attachment of the ligament. The own surgery technique is described.
We report a case of an unusual compact limy shading of the soft part in the lower leg, obviously caused by unphysique material the origin of which even retrospectively could not be clarified. Pathological compact limy shadings of the soft parts of the extremities are possible because of numerous reasons. Hereby the tissue calcination will be defined from the real ossifications and the direct exogene shades. Deficient knowledge of the pathophysiology often makes a preoperative difference very difficult with equivalent reoentgenological statements. The own difficulties in diagnosis of the case in question will be shown.
Malrotation of the distal femur could be important for the pathogenesis of the accidental dislocation of the patella. Most difficulties aries in the impossibility to prove and determine torsion deviations of the femur just as torsion deviations of the femur just as torsion deviations of other human bones with the methods at present available. With the syndrom of accidental dislocation of the patella often a series of promoting factore is combined. In animal experiences the consecutive alterations after producing artificial patella alta at the distal femur and at the patella bed with growing rabbits have been examined. It is found out that a real pathological torsion (inward torsion of the distal femur) is following.
The synthesis of the above mentioned decapeptide as a model for the active center of the inhibitor molecule is described. The Ki value of this peptide was found to be 4.7 X 10(-4)M. This Ki value differs from the Ki value of the Kunitz Inhibitor by a factor of 10(10).
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The initial binding of Cu2+ ot L-lysine, L-histidine, glycyl-histidine and histidyl-glycine in aqueous solutions was examined by 13C nuclear magnetic resonance spectroscopy. The measurements were carried out in a substantially improved way employing the pulse Fourier transform technique. Spectra of both high quality and resolution were obtained. Cu2+ complex formation with L-lysine occurred with the alpha-amino and carboxyl group attributable to the well expressed broadening effect of the 13C signals of the alpha-carbon atom and the carboxyl atom. The epsilon-amino group was not involved. Measurements of the Cu chelates using L-histidine and glycyl-histidine and histidyl-glycine confirmed the ambidentate nature of the histidine residue. It was concluded that an equilibrium exists between two Cu-complex species designated as histamine-like and histamine-like/glycine-like species. In the homogeneous histamine-like Cu complex, the Cu2+ is exclusively bound with 4 nitrogens, while in the other species one oxygen of the glycyl carboxyl group is involved in the Cu2+ binding. Blocking of this carboxyl groups by peptide bonding as found in histidyl-glycine favoured the formation of a Cu complex where the imidazole carbons of the histidyl residue were the most influenced species.
The screening phase of a multifactorial intervention study which is carried out under the direction of the WHO and the aim of which is the influence on mild forms of hypertension, hypercholesterolaemia and slightly disturbed glucose tolerance was supplemented by an electrocardiogram after work under the conditions of screening. The questionnaire contained in the investigation program for the statistical establishment of a typical angina pectoris after work according to Rose and the modified electrocardiographic test after work were tested concerning their evidence in the early recognition of a coronary sclerosis. As reference test served the Watt-step-test recommended by a group of experts of the WHO. An extensive correlation between screening after work and Watt-step-test was found. Questionnaire according to Rose and gradual load, however, had a smaller correspondence. The result of other investigations was that the distribution of the factors of risk does not give any clear reference to the existence of a latent coronary insufficiency.
The synthesis of the following 3 model peptides from the active center of the inhibitor molecule is described: (see article). The 3 peptides are split by trypsin with velocities increasing from (I) to (III). The following Ki values were determined: (I) Ki = 2.3 x 10(-2)M; (II) Ki = 4.9 x 10(-3)M; (III) Ki = 2.1 x 10(-3)M. These Ki values differ from the Ki values of the Kunitz inhibitor by a factor 10(11) to 10(12).
A simple isolation of melittin, apamin and MCD-peptide from bee venom is described. The peptides were separated using Sephadex G-50 and Biogel P-4 followed by preparative column chromatography using silicagel. Apamin and MCD-peptide were converted to the tetra-S-sulfonate derivatives by oxidative sulfitolysis. After reduction of these derivatives by mercaptoethanol followed by cautious air-reoxidation, the disulfide bridges can be reconstituted. The biological activities of the reoxidation products are 50 to 60% for apamin and 70 to 80% for MCD-peptide.
The synthesis of a [Glu5, Ala12, Ala18,-Ala21]sheep insulin-A-chain by condensation of 5 fragments on a polymer support is described. The 5 fragments Boc-Gly-Ile-Val-Glu(gammaOBut)-Glu(gammaOBut) (V), Boc-Cys(SiPr) (IV), Boc--Cys(SiPr)-Ala-Gly-Val (III), Boc-Cys(SiPr)-Ala-Leu-Tyr-Gln-Leu (II) and Boc-Glu(gammaOBut)-Ala--Tyr(Bzl)-Cys(SiPr)-N2H3 (I) were synthesized by conventional methods and coupled with dicyclohexylcarbodiimide/1-hydroxybenzotriazol (II, III, IV, V) and by the azide method (I) with coupling yields of 60-98% on an Ala-polymer. The failure sequence peptides were separated by ion exchange chromatography on DEAE-Sephadex and by chromatography on Biogel P4. The A-chain was obtained in 9% yield, which, after combinations with natural B-chain, gave insulin activities comparable to that obtained with natural A-chain. These results demonstrate that fragment condensation by the solid-phase method together with simple techniques for purification can be used for the synthesis of longer peptides.
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