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Studies on the cell cycle of Myxobacter AL-1
Authors:Wolfgang Hartmann  Ingrid Tan  Aloys Hüttermann  Hans Kühlwein
Affiliation:(1) Botanisches Institut der Universität Karlsruhe, Lehrstuhl I. Kaiserstr 12, D-7500 Karlsruhe, Federal Republic of Germany;(2) Forstbotanisches Institut der Universität Göttingen, D-3400 Göttingen, Federal Republic of Germany
Abstract:The properties of seven enzymes were studied in extracts from Myxobacter AL-1. The enzymes were isocitrate dehydrogenase (E.C. 1.1.1.42), succinate dehydrogenase (E.C. 1.3.99.1), alkaline phosphatase (E.C. 3.1.3.1), agr-glucosidase (E.C. 3.2.1.20), beta-glucosidase (E.C. 3.2.1.21), beta-galactosidase (E.C. 3.2.1.23), and N-acetyl-glucosaminidase (E.C. 3.2.1.30). Four of these enzymes: isocitrate dehydrogenase, agr-glucosidase, beta-glucosidase, and beta-galactosidase are cytosolic enzymes. Succinate dehydrogenase was found to be located on the cytoplasmic membrane system, whereas alkaline phosphatase and N-acetyl-glucosaminidase were considered as enzymes which bind the outer membranes resp. the cell wall. During the cell cycle, all enzymes have a pattern of discontinuous activity increase. Succinate dehydrogenase and isocitrate dehydrogenase exhibit a stepwise increase of activity, whereas the other enzymes follow the pattern of a peak enzyme.
Keywords:Myxobacteria  Myxobacter AL-1  Enzymes  Cytoplasmic membranes  Outer membranes  Isopycnic sedimentations  Metrizamide  Cell cycle  Step-enzymes  Peak-enzymes
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