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Home > Science & Mathematics > Biology, life sciences > Life sciences: general issues > Genetics (non-medical) > Molecular characterization and identification of antigen 32-5B6 as enzyme S-Adenosyl-L-Homocystein-Hydrolase from Xenopus laevis oocyte nuclei
Molecular characterization and identification of antigen 32-5B6 as enzyme S-Adenosyl-L-Homocystein-Hydrolase from Xenopus laevis oocyte nuclei

Molecular characterization and identification of antigen 32-5B6 as enzyme S-Adenosyl-L-Homocystein-Hydrolase from Xenopus laevis oocyte nuclei


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About the Book

Diplomarbeit aus dem Jahr 1996 im Fachbereich Biologie - Genetik / Gentechnologie, Note: keine Angabe, Eberhard-Karls-Universität Tübingen (Max-Planck-Institut für Entwicklungsbiologie, Tübingen), Veranstaltung: -, Sprache: Deutsch, Abstract: Molecular characterization and identification of antigen 32-5B6 as enzyme S-Adenosyl-L-Homocystein-Hydrolase from Xenopus laevis oocyte nuclei Claudia Mohl Diploma thesis in Biochemistry, Eberhard-Karls-University, Tübingen, 1996 and Max-Planck-Institut for Development Biology, Tübingen (Title and Abstract in english; Original work in german) Abstract: The aim of my diploma thesis work (1996) was molecular characterization and identification of late migrating antigen 32-5B6 on a molecular level. Antigen 32-5B6 is a protein that is distributed in cytoplasm during Blastula stage and transported into oocyte cell nuclei at Gastrula stage 12 during embryonic development of Xenopus laevis (Dreyer et al. 1982; 1983). To isolate cDNA sequences that encode the late migrating antigen 32-5B6, I screened, isolated and sequenced five cDNA clones from placques with positive antibody reaction from a Xenopus laevis ovar lambda zap II cDNA expression library. Sequence analysis showed that two cDNA clones encode the enzyme S-Adenosyl-Homocystein-L-Hydrolase (clone 10) from Xenopus laevis (Seery et al. 1994) and an isoform of this enzyme (clone 8). Molecular weight and IEP of S-Adenosyl-Homocystein-L-Hydrolase are nearly identical with those of antigen 32-5B6. To get further evidence in regard to sequence of antigen 32-5B6, proteins were isolated from original Xenopus laevis oocyte nuclei for protein microsequencing. For this reason I established a new protein purification strategy purifying proteins from original oocyte nuclei of Xenopus laevis proteom by means of anion-exchange chromatography and 2-dimensional gel electrophoresis. By means of western blot analysis I could detect two enzyme isoforms those IEPs lie in range between pH


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Product Details
  • ISBN-13: 9783640497591
  • Publisher: Grin Verlag
  • Publisher Imprint: Grin Verlag
  • Height: 210 mm
  • No of Pages: 94
  • Series Title: German
  • Sub Title: Molekulare Charakterisierung des Antigens 32-5B6 aus Oocytenkernen des Krallenfrosches Xenopus laevis
  • Width: 148 mm
  • ISBN-10: 3640497597
  • Publisher Date: 22 Dec 2009
  • Binding: Paperback
  • Language: German
  • Returnable: N
  • Spine Width: 6 mm
  • Weight: 181 gr


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Molecular characterization and identification of antigen 32-5B6 as enzyme S-Adenosyl-L-Homocystein-Hydrolase from Xenopus laevis oocyte nuclei
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Molecular characterization and identification of antigen 32-5B6 as enzyme S-Adenosyl-L-Homocystein-Hydrolase from Xenopus laevis oocyte nuclei
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