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  • Articles: DFG German National Licenses  (6)
Source
  • Articles: DFG German National Licenses  (6)
Material
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 4901-4906 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 53 (1984), S. 493-535 
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK; Malden, USA : Blackwell Science Ltd
    Journal of fish biology 64 (2004), S. 0 
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Longfinned eels Anguilla reinhardtii were captured by both fishery-dependent and independent sampling methods from three rivers in New South Wales, south-eastern Australia. Sex ratios, catch per unit effort and population age and total length structure were examined in three zones (fresh water and upper and lower tidal) in the Hacking, Hawkesbury and Clarence Rivers. Females were found in relatively high proportions in all zones, ranging from 97% in a freshwater (non-tidal) site down to 59% in a tidal site. Males were found primarily in tidal zones (only two of the 677 longfinned eels caught in non-tidal fresh water were males), with the greatest proportions being found in the brackish upper tidal areas. The mean number of fish captured per trap was higher in the fresh water and upper tidal zones than in the lower tidal zones. The mean ± s.e. age, 17·9 ± 0·3 years, and age range, 5–52 years for females were significantly higher than those of males 12·2 ± 0·4 years; range 5–22 years, which is typical of other anguillid species. Longfinned eels captured in fresh water were found be significantly larger and older than those in tidal zones due to the almost exclusive predominance of females.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Journal of fish biology 63 (2003), S. 0 
    ISSN: 1095-8649
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The sex and stage of gonadal development of longfinned river eels Anguilla reinhardtii, captured from nine river catchments in New South Wales, Australia, between 1999 and 2001, were determined macroscopically. Sex was verified by histology. Histology was also necessary, however, to accurately define stages of gonadal development, particularly in individuals 〈600 mm in total body length. Anguilla reinhardtii displayed asynchronous gamete development. The most advanced cells present in migrating male and female A. reinhardtii were spermatocytes and pre-vitellogenic oocytes, respectively. Gonadal development stages were positively correlated with body size in both sexes. Females, however, were significantly larger than males and their gonads matured over a broader size range. Size at sexual differentiation (42–60 cm for males and 50–76 cm for females) was much larger than for most other anguillids that have been studied, with the exception of the New Zealand longfinned eel Anguilla dieffenbachii. Corresponding with its large range in size at sexual differentiation was a relatively large range in size at migration for both males (44–62 cm) and females (74–142 cm).
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The three-dimensional structure of MerA from Bacillus sp. strain RC607 can be clearly divided into three parts: the two N-terminal regions (residues 1-166), the core (167-616), the equivalent of the glutathione reductase structure, and the C-terminal extension (residues 617-631). This partition is ...
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1617-4623
    Keywords: Key words Nodulation ; Rhizobium ; Lipo-chitin oligosaccharide ; NodF ; Fatty acid biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nodulation protein NodF of Rhizobium shows 25% identity to acyl carrier protein (ACP) from Escherichia coli (encoded by the gene acpP). However, NodF cannot be functionally replaced by AcpP. We have investigated whether NodF is a substrate for various E. coli enzymes which are involved in the synthesis of fatty acids. NodF is a substrate for the addition of the 4′-phosphopantetheine prosthetic group by holo-ACP synthase. The Km value for NodF is 61 μM, as compared to 2 μM for AcpP. The resulting holo-NodF serves as a substrate for coupling of malonate by malonyl-CoA:ACP transacylase (MCAT) and for coupling of palmitic acid by acyl-ACP synthetase. NodF is not a substrate for β-keto-acyl ACP synthase III (KASIII), which catalyses the initial condensation reaction in fatty acid biosynthesis. A chimeric gene was constructed comprising part of the E.coliacpP gene and part of the nodF gene. Circular dichroism studies of the chimeric AcpP-NodF (residues 1–33 of AcpP fused to amino acids 43–93 of NodF) protein encoded by this gene indicate a similar folding pattern to that of the parental proteins. Enzymatic analysis shows that AcpP-NodF is a substrate for the enzymes holo-ACP synthase, MCAT and acyl-ACP synthetase. Biological complementation studies show that the chimeric AcpP-NodF gene is able functionally to replace NodF in the root nodulation process in Vicia sativa. We therefore conclude that NodF is a specialized acyl carrier protein whose specific features are encoded in the C-terminal region of the protein. The ability to exchange domains between such distantly related proteins without affecting conformation opens exciting possibilities for further mapping of the functional domains of acyl carrier proteins (i. e., their recognition sites for many enzymes).
    Type of Medium: Electronic Resource
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