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Prokaryotic organism

Microbes are relatively simple in structure in that, when viewed under the light and electron microscope, few complex structures are observed. The general structure of prokaryotic cells is shown in Fig. 5.4 5). [Pg.262]

Prokaryotic organisms are metabolically the most diverse of all living systems and are responsible for most degradative processes in the biosphere. They can be grown [Pg.262]

Protein containing usual amino acids (enzymic activity) phospholipid polysaccharide [Pg.263]

Mucocomplex substances similar to Gram-positive lipid up to 20% of cell [Pg.263]

Not clearly distinct from call wall. Has a number of biochemical functions [Pg.263]

Hydroxylation of n-octane by cell extracts of Gordonia (Corynebacterium) sp. strain 7E1C (Cardini and Jurtshuk 1968), and of some strains of Acinetobacter calcoaceticus induced with -hexadecane (Asperger et al. 1981). [Pg.114]

Hydroxylation of long-chain carboxylic acids, amides, and alcohols—but not the esters or the corresponding alkanes—at the w-l, (0-2, and (o-3 positions by a soluble enzyme system from Bacillus megaterium (Miura and Fulco 1975 Narhi and Fulco 1986,1987). [Pg.114]

The transformation of benzene, toluene, naphthalene, biphenyl, and benzo[a]pyrene to the corresponding phenols (Trower et al. 1989) by Streptomyces griseus, and of phenanthrene by Streptomyces flavovirens to ( )tran5 -[95, 105 ]-9,10-dihydrodihydroxyphenanthrene with minor amounts of 9-hydroxyphenanthrene (Sutherland et al. 1990). [Pg.115]

The initial hydroxylation in the degradation of some terpenes the ring methylene group of camphor by Pseudomonas putida (Katagiri et al. 1968 Tyson et al. 1972 Koga et al. 1986), and the isopropylidene methyl group of linalool by a strain of P. putida (Ullah et al. 1990). [Pg.115]

The cytochrome P450j, is able to bring about the stereoselective epoxidation of cis-methylstyrene to the (IS,2R) epoxide (Ortiz de Montellano et al. 1991). [Pg.115]


Acetogenic bacterium Prokaryotic organism that uses carbonate as a terminal electron acceptor and produces acetic acid as a waste product. [Pg.601]

Heterologous expression systems comprise prokaryotic organisms (e.g., E. coli) and eukaryotic cells (e.g., yeast, HEK293, Xenopus oocytes), which are used to functionally express foreign genes or cDNAs. [Pg.583]

Although many prokaryotic organisms are single-celled (unicellular), some exist as multicellular filaments or collections of cells. Eukaryotic organisms may be unicellular or multicellular. Most eukaryotic cells are at least 5 pm in diameter, but many are much larger. The cells of most prokaryotes are small, ranging from 0.2 to 1 / m in diameter, but a few are much larger. [Pg.42]

Prokaryotic organisms Salmonella typhImurlumJA98, TA100 Gene mutation - - Pednekar et al. 1987... [Pg.163]

In this chapter we describe the basic principles involved in the controlled production and modification of two-dimensional protein crystals. These are synthesized in nature as the outermost cell surface layer (S-layer) of prokaryotic organisms and have been successfully applied as basic building blocks in a biomolecular construction kit. Most importantly, the constituent subunits of the S-layer lattices have the capability to recrystallize into iso-porous closed monolayers in suspension, at liquid-surface interfaces, on lipid films, on liposomes, and on solid supports (e.g., silicon wafers, metals, and polymers). The self-assembled monomolecular lattices have been utilized for the immobilization of functional biomolecules in an ordered fashion and for their controlled confinement in defined areas of nanometer dimension. Thus, S-layers fulfill key requirements for the development of new supramolecular materials and enable the design of a broad spectrum of nanoscale devices, as required in molecular nanotechnology, nanobiotechnology, and biomimetics [1-3]. [Pg.333]

Cell envelopes of prokaryotic organisms (archaea and bacteria) are characterized by the presence of two distinct components the cytoplasmic membrane, which constitutes the inner layer, and an outer supramolecular layered cell wall (for reviews see Ref. 4), which pre-... [Pg.333]

So far as is possible, the discussion in this chapter and in Chapters 37, 38, and 39 will pertain to mammalian organisms, which are, of course, among the higher eukaryotes. At times it will be necessary to refer to observations in prokaryotic organisms such as bacteria and viruses, but in such cases the information will be of a kind that can be extrapolated to mammalian organisms. [Pg.314]

Prokaryotic organisms Salmonella typhimurium (Ames assay) Gene mutation — FMC 1992b Durad 550B... [Pg.220]

Do these prokaryotic organisms display a primitive iron metabolism, in the sense that they form a relatively limited number of iron compounds, and are they accordingly good candidates to suspect as direct descendants of the primordial cell ... [Pg.154]

Before closing this chapter, we wish to remove any impression which the above description of anaerobic life might have left that the anaerobes are a few small groups of organisms. In fact there is immense variety of these prokaryote organisms, some... [Pg.235]

Also in the PP, associated with the CM, one can find the murein sacculus (for a review see [8]). This network is formed by the macromolecule pepti-doglycan, which confers the characteristic cell shape and provides the cell with mechanical protection. Peptidoglycans are unique to prokaryotic organisms and consist of a glycan backbone of N-acetylated muramic acid and N-acetylated glucosamine and cross-linked peptide chains [9-13]. [Pg.275]

Prokaryotic organisms Salmonella typhimurium TA82, TA102 Reverse mutation - Not tested De Flora etal. 1984 KCN... [Pg.108]

Prokaryotic organisms Escherichia coll Sd-4 (forward mutation)... [Pg.47]


See other pages where Prokaryotic organism is mentioned: [Pg.2134]    [Pg.279]    [Pg.826]    [Pg.43]    [Pg.44]    [Pg.327]    [Pg.84]    [Pg.383]    [Pg.352]    [Pg.376]    [Pg.161]    [Pg.106]    [Pg.114]    [Pg.138]    [Pg.40]    [Pg.340]    [Pg.60]    [Pg.93]    [Pg.275]    [Pg.310]    [Pg.137]    [Pg.138]    [Pg.66]    [Pg.114]    [Pg.115]    [Pg.117]    [Pg.118]    [Pg.129]    [Pg.65]    [Pg.225]    [Pg.180]    [Pg.388]    [Pg.56]    [Pg.58]   
See also in sourсe #XX -- [ Pg.44 , Pg.45 ]

See also in sourсe #XX -- [ Pg.4 , Pg.5 , Pg.18 , Pg.19 , Pg.234 ]




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