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  • Cellulase  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Intrinsic Fluorescence in Endoglucanase and Cellobiohydrolase from Trichoderma pseudokiningii S-38: Effects of pH, Quenching Agents, and Ligand Binding (1997)
    Springer
    The protein journal 16 (1997), S. 681-688 
    Details
    ISSN: 1573-4943
    Keywords: Cellulase ; endoglucanase ; cellobiohydrolase ; fluorescence ; tryptophan ; Trichoderma pseudokiningii S-38
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract To gain further insight into the difference in substrate specificity between endoglucanase and cellobiohydrolase, the intrinsic fluorescence properties of cellobiohydrolase I (CBH I) and endoglucanase I (EG I) from Trichoderma pseudokiningii S-38 were investigated. The results for the spectral characteristics, ligand binding and fluorescence quenching suggest that the fluorescence of two enzymes comes from tryptophan residues, and that tryptophan residue(s) may be involved in the function of the two enzymes. The results also suggest that the binding tryptophan in EG I may be more exposed to solvent than that in CBH I. This interpretation is supported by the observations that the effects of pH upon the fluorescence of EG I are greater than that of CBH I; spectral shifts are different in EG I and CBH I under various conditions, and fluorescence lifetime changes caused by cellobiose binding are larger for EG I than for CBH I.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026354403952
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  • 2
    Electronic Resource
    Electronic Resource
    Domain Structure and Conformation of a Cellobiohydrolase from Trichoderma pseudokiningii S-38 (1997)
    Springer
    The protein journal 16 (1997), S. 59-66 
    Details
    ISSN: 1573-4943
    Keywords: Cellulase ; cellobiohydrolase ; proteolysis ; core domain ; cellulose-binding domain ; fluorescence ; circular dichroism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A cellobiohydrolase (CBH) with a molecular mass of 66 kD was purified from Trichoderma pseudokiningii S-38. Papain digestion produced a 59- to 60-kD core domain with 54% of intact activity on crystalline cellulose and with full activity against soluble substrates. Digestion products also included two small peptides with molecular mass of about 3–4 kD, which are heavily glycosylated and difficult to purify; the mixed peptides displayed the capacity to disorganize the cellulose fiber. The sequencing results indicated that the intact enzyme had a blocked N-terminal and there was a 10-amino-acid sequence in the N-terminal of the core protein of Ser-Gly-Thr-Ala-Val-Thr-Cys-Leu-Ala-Asp. Fluoresence and circular dichroism properties indicated that the core protein has an independent conformation and is conformationally similar to intact enzyme, suggesting that the spectroscopic properties of the intact enzyme come from the core protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026394912245
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    Paper (German National Licenses)
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