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
    Cyclic AMP-dependent protein kinase in calf-snout epidermis (1986)
    Springer
    Archives of dermatological research 278 (1986), S. 367-371 
    Details
    ISSN: 1432-069X
    Keywords: Protein phosphorylation ; Cyclic AMP ; Cyclic AMP-dependent protein kinase ; Keratin polypeptide ; Calf-snout epidermis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The biochemical characteristics of cyclic AMP-dependent protein kinase in calf-snout epidermis were investigated. The activity of cyclic AMP-dependent protein kinase was higher in the lower layer than the upper layer of epidermis. The supernatant of homogenates of the lower layer of calf-snout epidermis was fractionated by DEAE-cellulose chromatography and contained two major peaks of protein kinase activity stimulated by cyclic AMP. This chromtographic pattern is similar to that referred to as Type I and Type II of cyclic AMP-dependent protein kinase in bovine muscle. Both peaks of cyclic AMP-dependent protein kinase in calf-snout epidermis could phosphorylate keratin polypeptides in vitro. The phosphorylation reaction was activated by cyclic AMP and inhibited by a heat-stable inhibitor of cyclic AMP-dependent protein kinase. When Type II enzyme of cyclic AMP-dependent protein kinase was incubated with [γ-32P]ATP in the absence of substrates, such as histone or keratin polypeptides, the 54,000 dalton protein was phosphorylated and this autophosphorylation was inhibited by the addition of 10 μM cyclic AMP. These results suggest that cyclic AMP-dependent protein kinase in calf-snout epidermis has properties similar to those in bovine muscle and plays an important role in the phosphorylation of keratin polypeptides in calf-snout epidermis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418164
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Activity losses among T4 lysozyme variants after adsorption to colloidal silica (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 58 (1998), S. 658-662 
    Details
    ISSN: 0006-3592
    Keywords: T4 lysozyme ; silica nanoparticles ; synthetic enzyme variants ; surface-induced conformational change ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Maintaining a specific molecular conformation is essential for the proper functioning of an enzyme. A substantial loss of catalytic activity can occur from the displacement caused by even a single amino acid substitution. Activity may also be lost as an enzyme undergoes a conformational change during adsorption. In this study, we investigated the effect of thermostability on the activities of three T4 lysozyme variants after adsorption to 9 nm colloidal silica particles. Less-stable T4 lysozyme variants lost more activity after adsorption than did more stable variants, apparently because they experienced more extensive structural alteration. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58: 658-662, 1998.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    Letters to the editor (1983)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 18 (1983), S. 494-496 
    Details
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/oms.1210181108
    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...