By A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.)
This quantity in a research-level sequence covers assorted elements of microbial body structure and biochemistry together with inositol metabolisms in yeasts, bacterial adhesion, natural acids, the bacterial flagellum and the mechanical behaviour of bacterial mobilephone partitions. it truly is meant to be of use to microbiologists, biochemists and biotechnologists. different similar works during this sequence are volumes 29, 30 and 31.
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This quantity in a research-level sequence covers varied facets of microbial body structure and biochemistry together with inositol metabolisms in yeasts, bacterial adhesion, natural acids, the bacterial flagellum and the mechanical behaviour of bacterial telephone partitions. it truly is meant to be of use to microbiologists, biochemists and biotechnologists.
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Extra info for Advances in Microbial Physiology, Vol. 24
1975b; Osumi and Sato, 1978) it was suggested that both catalase and alcohol oxidase were structural elementsof the crystalloids, contained in peroxisomes of methanolgrown Kloeckera sp. 2201. Tilting experiments with cryosections of this organism showed that the different crystalline patterns observed in the peroxisomal matrix were in fact artificial images all of which could be accounted for by superposition of two different types of particles arranged alternately in a tetragonal lattice. , 1979).
Similar patterns of synthesis were observed for catalase and formaldehyde dehydrogenase (Fig. 12). The specific activity of formate dehydrogenase remained low during the first hours of cultivation after the transfer but increased during later stages of growth. The enzyme profiles obtained after transfer of cells into methylamine-containing media were largely similar in the two organisms studied. Transfer of H. polymorpha and C . utilis from glucose plus ammonium sulphate into glucose plus methylamine media was followed by ultrastructural changes in the cells (Zwart et a / .
1981a). Furthermore, when H. polymorpha was grown under methanol-limitation in chemostat culture, the ratio of alcohol oxidase and catalase varied considerably with the growth rate (van Dijken, 1976). Yet, under these conditions, the peroxisomes were completely crystalline, irrespective of the growth rate of these cells. , 1976,1979a)it is difficult to envisage that these organellescan be composed of the two enzymes in a fixed 1:l ratio. The distribution of alcohol oxidase and catalase activities in completely crystalline peroxisomes present in chemostat-grown cells of H.
Advances in Microbial Physiology, Vol. 24 by A.H. Rose, J. Gareth Morris and D.W. Tempest (Eds.)