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  • Cystinyl  (1)
  • metallopeptidase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Homology of functionally diverse proteins (1977)
    Springer
    Journal of molecular evolution 9 (1977), S. 349-361 
    Details
    ISSN: 1432-1432
    Keywords: Disulphide ; Cystinyl ; Homologous Proteins ; Functionally Diverse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Disulphide-rich proteins of widely differing functions were aligned with the aid of their half-cystinyl residues. This led to the grouping of ribonuclease, phospholipase A, lysozyme, snake venom toxins, bee and scorpion venom peptides, and the plant proteins potatoe carboxypeptidase inhibitor, ragweed pollen allergen, mistletoe toxins and pineapple sulfhydryl protease inhibitor into one super-family of proteins. Very few deletions/insertions were needed to effect alignment and probabilities were calculated for random occurrence of the matches that were found.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01796098
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The amino-terminal sequence ofStreptomyces griseus carboxypeptidase (1985)
    Springer
    The protein journal 4 (1985), S. 141-149 
    Details
    ISSN: 1573-4943
    Keywords: metallopeptidase ; amino-terminal sequence ; homology ; sequencer background
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The amino-terminal sequence of carboxypeptidase fromStreptomyces griseus was determined using a new protocol for automatic Edman degradation that reduced background noise. The sequence of the first 48 residues is: Asp-Phe-Pro-Pro-Ala-Asp-Ser-Arg-Tyr-His-Asn-Tyr-Ala-Glu-Met-Asn-Ala-Ala-Ile-Asp-Ala-Arg-Ile-Ala-Ala-Asn-Pro-Ser-Ile-Met-Ser-Lys-Arg-Val-Ile-Gly-Lys-Thr-Tyr-Gln-Gly-(Arg)-Asp-Val-Ile-Ala-Val-Lys, which is homologous to that of other zinc-containing carboxypeptidase from vertebrate and invertebrate sources.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025260
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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