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  • 1
    Digitale Medien
    Digitale Medien
    Biogenetic-type chemistry of the indole alkaloids (1969)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 91 (1969), S. 5872-5874 
    Details
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ja01049a031
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  • 2
    Digitale Medien
    Digitale Medien
    Mechanism of indole alkaloid biosynthesis. The Corynanthe-Strychnos relationship (1969)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 91 (1969), S. 4932-4933 
    Details
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ja01045a065
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  • 3
    Digitale Medien
    Digitale Medien
    Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from lupin root nodules (1992)
    Springer
    Plant molecular biology 19 (1992), S. 465-472 
    Details
    ISSN: 1573-5028
    Schlagwort(e): aspartate aminotransferase ; cDNA ; nodule ; lupin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Two isoenzymic forms of aspartate aminotransferase are present in the plant fraction of developing lupin root nodules. One of these forms, aspartate aminotransferase-P2 (AAT-P2), increases dramatically with the onset of biological nitrogen fixation and is associated with the assimilation of ammonia by the plant in the Rhizobium-legume symbiosis. A day 18 lupin nodule cDNA library in the λZapII vector was immunoscreened with a monoclonal antibody specific for AAT-P2 and yielded two near-full-length 1700 bp clones. These clones were sequenced. Amino acid sequences from three peptides derived from immunopurified AAT-P2 were aligned, and showed 100% homology with the amino acid sequence deduced from the cDNA clones. The DNA sequence showed 50% homology with AAT sequences from a range of animal sources. Conversion of the clones to the phagemid form allowed their expression in Escherichia coli where both exhibited enzyme activity that could be immunoprecipitated with AAT-P2-specific monoclonal antibodies. Western blot analysis revealed protein moieties with molecular masses of 39, 43, 45 and 55 kDa. The 5′ end of the clones coded for a hydrophobic leader sequence of about 50 amino acids indicative of a targeting sequence and consistent with the plastid localisation of nodule AAT-P2.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00023394
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  • 4
    Digitale Medien
    Digitale Medien
    Constant external work cycle exercise – the performance and metabolic effects of all-out and even-paced strategies (1996)
    Springer
    European journal of applied physiology 75 (1996), S. 22-27 
    Details
    ISSN: 1439-6327
    Schlagwort(e): Key words Constant work   ;   Muscle action speed   ;    Power-velocity relationship   ;   Pacing strategies
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract The purpose of the present study was to establish whether the performance of an all-out sprint could be replicated and the metabolic responses moderated in two further trials involving pre-set constant average pedalling rates. A total of 24 subjects (12 males and 12 females) completed a 30-s high-speed maximal all-out effort on a cycle ergometer against an applied resistance equal to 7.5% of their body mass. On two further occasions the applied resistance was increased so that the external work of the all-out effort could be replicated by adopting a pre-determined constant average pedal rate. When the required pedal rate was within the range of 60–90 rev  ·  min−1 the subjects were able to maintain the rate for the full 30-s and so could replicate the external work of the all-out effort. They were unable to sustain a faster constant rate within the range of 97–150 rev  ·  min−1 for the full 30 s, resulting in ≈7% less external work being achieved (P 〈  0.05). A lower level of fatigue, reflected by less of a reduction in peak power output in a subsequent 6-s sprint (P 〈 0.05), arose as a result of similar work produced under constant paced conditions compared with the all-out effort. Also, post-exercise blood lactate, pH and ammonia were less disturbed (P 〈 0.05) following the paced trial compared with similar work produced in the all-out effort. A possible explanation for these findings is that there may be a partial sparing of some type II fibres as a consequence of an initial submaximal intensity of exercise during the paced trial.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004210050121
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  • 5
    Digitale Medien
    Digitale Medien
    The effect of crystallinity on chain mobility and free volume in the amorphous regions of a miscible polycarbonate/polyester blend (1994)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 32 (1994), S. 1237-1247 
    Details
    ISSN: 0887-6266
    Schlagwort(e): Polycarbonate ; ThermX ; semicrystalline polyester ; positron lifetimes ; miscible blends ; free volume ; Chemistry ; Polymer and Materials Science
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie , Physik
    Notizen: Homopolymers and blends of polycarbonate/ThermX have been investigated by differential scanning calorimetry, dynamic mechanical analysis, density measurements, and positron annihilation lifetime spectroscopy. The study focuses on the chain mobility and free volume in the amorphous miscible regions of the blends and how this mobility and free volume are affected by increasing crystallinity. It is proposed that judicious annealing, which results in increasing crystallinity (while avoiding ageing or transesterification), induces a constraint on the amorphous region leading to an increase in Tg and coalescence of free volume sites. © 1994 John Wiley & Sons, Inc.
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/polb.1994.090320711
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