Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase (1991)
    Springer
    The protein journal 10 (1991), S. 69-73 
    Details
    ISSN: 1573-4943
    Keywords: Amino acid sequence ; post translational modification ; peptide analysis ; isozymes ; high-performance liquid chromatography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The class III human liver alcohol dehydrogenase, identical to glutathione-dependent formaldehyde dehydrogenase, separates electrophoretically into a major anodic form (χ1) of known structure, and at least one minor, also anodic but a slightly faster migrating form (χ2). The primary structure of the minor form isolated by ion-exchange chromatography has now been determined. Results reveal an amino acid sequence identical to that of the major form, suggesting that the two derive from the same translation product, with the minor form modified chemically in a manner not detectable by sequence analysis. This pattern resembles that for the classical alcohol dehydrogenase (class I). Hence, the χ1/χ2 multiplicity does not add further primary forms to the complex alcohol dehydrogenase system but shows the presence of modified forms also in class III.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024657
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    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
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...