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'Biological Activity' in keywords Facet   section ZfN Section C  [X]
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1988 (1)
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1Author    AngelM. RelimpioRequires cookie*
 Title    Structure and Anticholinesterase Activity of Series of Ethyl Substituted Phenyl Methylphosphonates  
 Abstract    Thirty derivates from substituted-phenyl-ethyl methylphosphonates have been synthesized and their inhibiting power of acetyl-cholinesterase have been examined in vitro and in vivo. The cor­ relation between inhibition of the enzyme and electrophylic power of the substituent of the phenyl group was excellent, but when this group contains two substituents, steric factors appear to operate. The activity of these compounds has been demonstrated to be higher than their phosphate analogs. 
  Reference    (Z. Naturforsch. 32c, 760 [1977]; received June 13 1977) 
  Published    1977 
  Keywords    Cholinesterase, Methylphosphonates, Inhibitors, Biological Activity 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0760.pdf 
 Identifier    ZNC-1977-32c-0760 
 Volume    32 
2Author    Irene UrbaschRequires cookie*
 Title    Transformationen von trans-2-Hexenal durch Botrytis cinerea PERS. als Entgiftungsmechanismen Transformations of trans-2-H exenal by Botrytis cinerea PERS. as Detoxification M echanisms  
 Abstract    The m etabolization of /rö«5-2-hexenal — one of the main components of plant wound gases with antibiotic activity — was investigated for 5 different isolates of Botrytis cinerea PERS. The transform ation products as well as the kinetics of their formation were analyzed. Isolates exclusively mycelium forming (Be 1 and Be 13) transform ed rr-2-hexenal into tr-2-hexenol, while sporulating isolates (Be 3, Be 9 and Be 10) converted rr-2-hexenal to hexanol-1. Basically the m etabolization of rr-2-hexenal proceeded in the same way via the aqueous phase as in the gas phase. The transform ation products fr-2-hexenol and hexanol-1 showed significantly lower toxicity against the tested B. cinerea isolates than ?/--2-hexenal. In each isolate the end product of tr-2-hexenal conversion had the weakest inhibitory activity. The transform ation reactions thus repre­ sent detoxification mechanisms for these fungi. 
  Reference    Z. Naturforsch. 42c, 64—68 (1987); received August 26/November 12 1986 
  Published    1987 
  Keywords    Botrytis cinerea, fr-2-Hexenal Conversion, Biological Activity, Detoxification 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0064.pdf 
 Identifier    ZNC-1987-42c-0064 
 Volume    42 
3Author    Dagmar Denklau, Wolfgang Köhnlein, G. Erd Lüders, Joachim SteilmachRequires cookie*
 Title    Isolation and Fast Purification o f Neocarzinostatin by FPLC-Ion Exchange Chromatography  
 Abstract    Neocarzinostatin, a highly toxic antitum or protein containing an essential nonprotein Chromo­ phore, can be isolated and purified from culture filtrates o f Streptomyces carzinostaticus. Usually a lengthy procedure of up to 60 h is necessary for the isolation, including several chromatographic steps partly under conditions which favour inactivation of the drug by release of chrom ophore. We describe a new method yielding practically clinical grade N eocarzinostatin from crude extracts in 20 min. This very fast and reproducible m ethod was m ade possible by using a Mono Q anion exchange column filled with m onodisperse gel m aterial which has been recently developed. 
  Reference    Z. Naturforsch. 38c, 939 (1983); received July 1/August 31 1983 
  Published    1983 
  Keywords    Zinostatin, Antitumor Antibiotic, Fast Purification, Biological Activity, Protein-H PLC 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0939.pdf 
 Identifier    ZNC-1983-38c-0939 
 Volume    38 
4Author    Frank Beise, Harald Labischinski, Hans BradaczekRequires cookie*
 Title    On the Relationships between Molecular Conformation, Affinity towards Penicillin-Binding Proteins, and Biological Activity of Penicillin G-Sulfoxide  
 Abstract    The binding capacity of penicillin G-sulfoxide towards the penicillin-binding proteins (PBP) of Staphylococcus aureus H was studied. The sulfoxide and its parent compound, penicillin G, differ only in two aspects, the sulfur-bound oxygen and an altered conformation of the five-membered thiazolidine-ring system. These minor alterations of the penicillin structure resulted in a drastical decrease of binding activity (about two orders of magnitude) of the sulfoxide derivative towards its target enzymes. Furthermore, the sulfoxide did not exhibit the selectivity of subinhibitory doses for PBP 3, as could be observed for penicillin G. The biological consequences of this behaviour were monitored via growth curves, uptake of cell wall label, and analysis of the cell wall. Binding studies revealed that comparable growth inhibi-tion and impairment of cell wall label uptake were achieved by at least a 100-fold higher penicillin G-sulfoxide concentration, compared to its parent compound. In cell wall analysis, the application of high doses of the antibiotics, i.e. nearly saturated PBP, verified the above mentioned observation. Surprisingly, small but significant differences in cell wall composition occurred using subinhibitory doses, probably due to the altered affinity towards PBP 3, supporting the hypothesis of an important role of this PBP in peptidoglycan transpeptida-tion. 
  Reference    Z. Naturforsch. 43c, 656—664 (1988); received March 25/June 28 1988 
  Published    1988 
  Keywords    Penicillin G, Penicillin G-Sulfoxide, Penicillin-Binding Proteins, Biological Activity, Structure Activity Relationships 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0656.pdf 
 Identifier    ZNC-1988-43c-0656 
 Volume    43