Biomedical subjects

G Wahler

Publications and source records attributed to G Wahler.

6 recordsLinked to original sources

PubMed1996

[Concomitant injuries after upper ankle joint dislocations].

Functional treatment with the Air Stirrup Ankle Brace recommended by C. N. Stover in 1979 can reduce pathological inversion of the ankle joint. In our retrospective study of 109 patients treated by this kind of ankle brace we found 96 patients (88%) with excellent results. Only 13 patients (12%) reported moderate to good results. To detect and characterize their painful conditions of ankles we did a clinical, radiological and MRI-Investigation. In only 2 cases we found a moderate instability after clinical investigation, anterior stress roentgenogram and talar tilt. By using the MRI-investigation 1.0 Tesla with a 512 x 360 Matrix we could find 10 cases with osteochondral lesions of the ankle. In 7 cases there was separated ossicle in the fibulotalar joint, in 1 case we detected a fracture of the processus anterior tali, in another case we could see a posttraumatic lesion of the talus and calcaneus with bone bruise and at least one osteochondral fracture of the distal tibia. The capability of the MRI to detect particularly osteo-chondral lesions of the talus and the tibiofibular joint was shown in 10 of 13 cases. Therefore we recommend to do an MRI-investigation on all patients after ankle sprain if there are painful conditions within the ankle after conservative treatment.

Adult↗

PubMed1990

Crystallization and preliminary X-ray studies of D-serine dehydratase from Escherichia coli.

Single crystals of D-serine dehydratase from Escherichia coli complexed with 3-amino-2-hydroxypropionate have been obtained from ammonium sulfate solution (pH 7.0) by vapor diffusion. The crystals belong to the trigonal space group P3(1) or P3(2) with a = b = 81.3 A and c = 58.4 A. The asymmetric unit cell contains one protein molecule with Mr = 48,289. The crystals diffract to at least 3.0 A resolution and are suitable for X-ray structure analysis.

Crystallization↗

PubMed1989

Evidence that 31P NMR is a sensitive indicator of small conformational changes in the coenzyme of aspartate aminotransferase.

The pH dependence of 31P-NMR spectra of pig cytosolic aspartate aminotransferase, containing either N-(5'-phosphopyridoxyl)-L-aspartate or pyridoxal 5'-deoxymethylenephosphonate in place of the normal coenzyme pyridoxal 5'-phosphate, has been analysed. The chemical shifts of phosphopyridoxylaspartate and of pyridoxal 5'-deoxymethylenephosphonate model Schiff base in free solution show pK values of 6.3 and 7.4, attributable to the second deprotonation step of phosphate and phosphonate, respectively. However, these compounds behave very differently when bound to apoaspartate aminotransferase. 31P-NMR spectra of these enzyme derivatives indicate that the phosph(on)ate group remains dianionic throughout the pH range 4-8.5. A clear correlation between apparent pK values obtained from spectrophotometric titration of the coenzyme chromophore and those obtained by 31P NMR indicates that the same ionisation is being reported by both methods. The data are interpreted, on the basis of available crystallographic structures of chicken mitochondrial aspartate aminotransferase, to indicate that in each case the alteration in 31P chemical shift results from a conformational change in the coenzyme 5' side chain, in which one of the structures involves a near-eclipsed pair of bonds. Such a stressed conformation produces slight alterations in bond angles around the phosphorus atom, which in turn cause the observed change in 31P chemical shift. The evidence is taken to indicate that in this case 31P NMR is a sensitive reporter of stress in enzyme-bound pyridoxal 5'-phosphate and its derivatives.

Animals↗

PubMed1989

Purification and characterization of dihydropyrimidine dehydrogenase from pig liver.

Dihydropyrimidine dehydrogenase was isolated from cytosolic pig liver extracts and purified 3100-fold to apparent homogeneity. Purification made use of ammonium sulfate fractionation, precipitation with acetic acid and chromatography on DEAE-cellulose and 2',5'-ADP-Sepharose with 28% recovery of total activity. The native enzyme has a molecular mass of 206 kDa and is apparently composed of two similar, if not identical, subunits. Proteolytic cleavage reveals two fragments with apparent molecular masses of 92 kDa and 12 kDa. The C-terminal 12-kDa fragment seems to be extremely hydrophobic. The enzyme contains tightly associated compounds including four flavin nucleotide molecules and 32 iron atoms/206-kDa molecule. The iron atoms are probably present in iron-sulfur centers. The flavins released from the enzyme were identified as FAD and FMN in equal amounts. An isoelectric point of 4.65 was determined for the dehydrogenase. Apparent kinetic parameters were obtained for the substrates thymine, uracil, 5-aminouracil, 5-fluorouracil and NADPH.

Animals↗

PubMed1989

[Management of hip fractures using a dynamic hip screw].

Authors describe the history of the dynamic hip screw and analyse the hip fracture. The operative technique of the DHS is described in details. In an analysis of the material of the Wilhelminenspital it is stressed that in the last years the DHS became dominant in the treatment of hip fractures. The treatment of four different types of fractures with DHS is demonstrated. The method is compared with other methods suitable for the treatment of hip fractures and it is stated that the less complications can be expected from the use of the DHS. On the basis of this comparison it is shown that the DHS is worthy to occupy a decisive place in the treatment of hip fractures.

Aged↗

PubMedDate not supplied

Cardiac sarcolemmal substrate of the cGMP-dependent protein kinase.

Cardiac sarcolemmae from guinea pig ventricles were purified and incubated with cGMP-dependent protein kinase. In the presence of the purified kinase plus 10(-5) M cGMP or 8-Br-cGMP, a protein of approximately 50 kD, (Kilodalton) was phosphorylated. This membrane-associated cGMP-dependent protein kinase substrate is similar in MW to the regulatory subunit of the cAMP-dependent protein kinase, which is known to be a substrate for the cGMP-dependent protein kinase. Thus, this substrate, the identity of which remains to be proven, may be a possible mediator of cGMP-mediated control of cardiac function.

Animals↗