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  • 1
    Electronic Resource
    Electronic Resource
    Modification of tomato andAspergillus niger pectinesterases with diethyl pyrocarbonate (1996)
    Springer
    The protein journal 15 (1996), S. 127-130 
    Details
    ISSN: 1573-4943
    Keywords: Pectinesterase ; tomato ; Aspergillus niger ; histidine modification ; diethyl pyrocarbonate ; inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The role of histidine residues in pectinesterases was evaluated by monitoring the sensitivity to modification with diethyl pyrocarbonate in the tomato andAspergillus niger enzymes. Different and incomplete losses of enzyme activity were obtained. Inactivation of the enzymes was proportional to the histidine content (two in the tomato T1 form, six in theAspergillus form), suggesting that accessible histidine residues do not have active-site functions in these pectinesterases, but contribute to the overall structural stability. Lack of His roles in common between the enzyme forms is in agreement with the structures of pectinesterases having no conserved His residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01887393
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Primary structure of the hemolglobin β-chain of Rose-ringed Parakeet (Psittacula krameri) (1989)
    Springer
    The protein journal 8 (1989), S. 481-486 
    Details
    ISSN: 1573-4943
    Keywords: β-chain ; hemoglobin ; rose-ringed parakeet ; structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The primary structure of Rose-ringed Parakeet hemoglobin β-chain was established, completing the analysis of this hemoglobin. Comparisons with other avian β-chains show variations smaller than those for the corresponding α-chains. There are 11 amino acid exchanges in relationship to the only other characterized psittaciform β-chain, and a total of 35 positions are affected by differences among all avian β-chains analyzed (versus 61 for the α-chains). At three positions, the Psittacula β-chain has residues unique to this species. Three α1β1 contacts are modified, by substitutions at positions β51, β116, and β125.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01026432
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Primary structure of the hemoglobin α-chain of rose-ringed parakeet (Psittacula krameri) (1988)
    Springer
    The protein journal 7 (1988), S. 561-569 
    Details
    ISSN: 1573-4943
    Keywords: hemoglobin ; structural analysis ; molecular evolution ; avian relationships
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structure of the hernoglobin α-chain of Rose-ringed Parakeet was determined by sequence degradations of the intact subunit, the CNBr fragments, and peptides obtained by digestion with staphylococcal Glu-specific protease and trypsin. Using this analysis, the complete α-chain structure of 21 avian species is known, permitting comparisons of the protein structure and of avian relationships. The structure exhibits differences from previously established avian α-chains at a total of 61 positions, five of which have residues unique to those of the parakeet (Ser-12, Gly-65, Ser-67, Ala-121, and Leu-134). The analysis defines hemoglobin variation within an additional avian order (Psittaciformes), demonstrates distant patterns for evaluation of relationships within other avian orders, and lends support to taxonomic conclusions from molecular data.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024874
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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