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  • aldehyde dehydrogenase  (3)
  • Key words: Video-assisted thoracoscopic surgery — Thoracolumbar junction — Spinal lesions  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Video-assisted thoracoscopic treatment of spinal lesions in the thoracolumbar junction (1997)
    Springer
    Surgical endoscopy and other interventional techniques 11 (1997), S. 1189-1193 
    Details
    ISSN: 1432-2218
    Schlagwort(e): Key words: Video-assisted thoracoscopic surgery — Thoracolumbar junction — Spinal lesions
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Background: The endoscopic treatment of spinal lesions in the thoracolumbar junction (T11–L2) poses a great challenge to the surgeon. From November 1, 1995 to December 31, 1996, we successfully used a combination of video-assisted thoracoscopy and conventional spinal instruments to treat 38 patients with anterior spinal lesions. Twelve of them had lesions in the thoracolumbar junction. Methods: The so-called extended manipulating channel method was used to perform vertebral biopsy, discectomy, decompressive corpectomy, interbody fusions, and/or internal fixations in these patients. The size of the thoracoscopic portals was greater than usual in order to allow conventional spinal instruments and a thoracoscope to enter the chest cavity freely and be manipulated by techniques similar to those used in standard open surgical procedures. In this series, the procedures were performed by using either a three-portal approach (2.5–3.5 cm) or a modified two-portal technique involving a 5–6 cm larger incision and a small one for introducing the scope. Results: None of the operations resulted in injury to the great vessels, internal organs, or spinal cord. The total time for the operation ranged from 1.5 to 4.5 h (average, 3); and the total blood loss ranged from 50 to 3000 cc (average, 1050). One patient was converted to an open procedure due to severe pleural adhesion. Complications included two instances of transient intercostal neuralgia, one superfical wound infection, and one residual pneumothorax. Conclusions: The video-assisted technique with the extended manipulating channel method presented in this report simplifies thoracoscopic spinal surgery in the thoracolumbar junction and makes it easier. It avoids division of the diaphragm, removal of the rib, and wide spread of the intercostal space, and it allows greater control of intraoperative vessel bleeding. Using this technique, the number of portals required during the procedure can be reduced. In addition, the technique reduces the endoscopic materials required, thus lowering overall cost. It is an effective and promising approach.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004649900566
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Human stomach alcohol and aldehyde dehydrogenases (ALDH): A genetic model proposed for ALDH III isozymes (1988)
    Springer
    Biochemical genetics 26 (1988), S. 343-360 
    Details
    ISSN: 1573-4927
    Schlagwort(e): alcohol dehydrogenase ; aldehyde dehydrogenase ; genetic model ; human stomach ; isozyme
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. γγ ADH isozymes were expressed predominantly in the mucosal layer of the stomach, whereas ββ isozymes were in the muscular layer. In the 56 gastroendoscopic mucosal biopsies examined, the homozygous ADH3 1-1 phenotype was found in 75% of the samples, and the heterozygous ADH3 2-1 phenotype in 25%. Accordingly, the gene frequencies of the allelesADH 3 1 andADH 3 2 were calculated to be 0.88 and 0.12, respectively. Using a modified agarose isoelectric focusing procedure, gastric ALDH I, ALDH II, and up to five ALDH III forms could be clearly resolved. The ALDH III isozymes accounted for more than 80% of the total ALDH activities in gastric mucosa and exhibitedK m values in the millimolar range for propionaldehyde atpH 9.0. Forty-five percent of the 55 gastroendoscopic biopsies studied lacked ALDH I isozyme. The complex gastric ALDH III isozyme phenotypes seen in these biopsies fall into three patterns. They can be interpreted by a genetic hypothesis, based on a dimeric molecule, in which there are two separate genes,ALDH 3a andALDH 3b, with theALDH 3b locus exhibiting polymorphism. The homozygous phenotypes ALDH3b 1-1 and ALDH3b 2-2 were found to be 4 and 76%, respectively, and the heterozygous ALDH3b 2-1 phenotype 20%, of the total. Therefore, the allele frequencies forALDH 3b 1 andALDH 3b 2 were calculated to be 0.14 and 0.86, respectively. Several lines of biochemical evidence consistent with this genetic model are discussed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02401788
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  • 3
    Digitale Medien
    Digitale Medien
    Human stomach alcohol and aldehyde dehydrogenases (ALDH): A genetic model proposed for ALDH III isozymes (1988)
    Springer
    Biochemical genetics 26 (1988), S. 343-360 
    Details
    ISSN: 1573-4927
    Schlagwort(e): alcohol dehydrogenase ; aldehyde dehydrogenase ; genetic model ; human stomach ; isozyme
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Isozyme phenotypes of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) from human gastroendoscopic as well as surgical gastric biopsies were determined by starch gel electrophoresis and agarose isoelectric focusing. γγ ADH isozymes were expressed predominantly in the mucosal layer of the stomach, whereas ββ isozymes were in the muscular layer. In the 56 gastroendoscopic mucosal biopsies examined, the homozygous ADH3 1-1 phenotype was found in 75% of the samples, and the heterozygous ADH3 2-1 phenotype in 25%. Accordingly, the gene frequencies of the allelesADH 3 1 andADH 3 2 were calculated to be 0.88 and 0.12, respectively. Using a modified agarose isoelectric focusing procedure, gastric ALDH I, ALDH II, and up to five ALDH III forms could be clearly resolved. The ALDH III isozymes accounted for more than 80% of the total ALDH activities in gastric mucosa and exhibitedK m values in the millimolar range for propionaldehyde atpH 9.0. Forty-five percent of the 55 gastroendoscopic biopsies studied lacked ALDH I isozyme. The complex gastric ALDH III isozyme phenotypes seen in these biopsies fall into three patterns. They can be interpreted by a genetic hypothesis, based on a dimeric molecule, in which there are two separate genes,ALDH 3a andALDH 3b, with theALDH 3b locus exhibiting polymorphism. The homozygous phenotypes ALDH3b 1-1 and ALDH3b 2-2 were found to be 4 and 76%, respectively, and the heterozygous ALDH3b 2-1 phenotype 20%, of the total. Therefore, the allele frequencies forALDH 3b 1 andALDH 3b 2 were calculated to be 0.14 and 0.86, respectively. Several lines of biochemical evidence consistent with this genetic model are discussed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00554070
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Kinetic evidence for human liver and stomach aldehyde dehydrogenase-3 representing an unique class of isozymes (1989)
    Springer
    Biochemical genetics 27 (1989), S. 321-331 
    Details
    ISSN: 1573-4927
    Schlagwort(e): aldehyde dehydrogenase ; isozyme ; human stomach and liver ; kinetic property
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Substrate and coenzyme specificities of human liver and stomach aldehyde dehydrogenase (ALDH) isozymes were compared by staining with various aldehydes including propionaldehyde, heptaldehyde, decaldehyde, 2-furaldehyde, succinic semialdehyde, and glutamic γ-semialdehyde and with NAD+ or NADP+ on agarose isoelectric focusing gels. ALDH3 isozyme was isolated from a liver via carboxymethyl-Sephadex and blue Sepharose chromatographies and its kinetic constants for various substrates and coenzymes were determined. Consistent with the previously proposed genetic model for human ALDH3 isozymes (Yinet al., Biochem. Genet. 26:343, 1988), a single liver form and multiple stomach forms exhibited similar kinetic properties, which were strikingly distinct from those of ALDH1, ALDH2, and ALDH4 (glutamic γ-semialdehyde dehydrogenase). A set of activity assays using various substrates, coenzymes, and an inhibitor to distinguish ALDH1, ALDH2, ALDH3, and ALDH4 is presented. As previously reported in ALDH1 and ALDH2, a higher catalytic efficiency (V max/K m) for oxidation of long-chain aliphatic aldehydes was found in ALDH3, suggesting that these enzymes have a hydrophobic barrel-shape substrate binding pocket. Since theK m value for acetaldehyde for liver ALDH3, 83 mM, is very much higher than those of ALDH1 and ALDH2, ALDH3 thus represents an unique class of human ALDH isozymes and it appears not to be involved in ethanol metabolism.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00554167
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