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  • Clathrin-CAPs complex  (1)
  • Selective absorption  (1)
  • phospholipase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Emerging functional roles for the glycosyl-phosphatidylinositol membrane protein anchor (1990)
    Springer
    The journal of membrane biology 117 (1990), S. 1-10 
    Details
    ISSN: 1432-1424
    Keywords: phospholipase ; cell surface polarity ; lateral mobility ; hormone action
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Conclusion Experimental evidence has accumulated over the past few years to suggest that the GPI protein anchor may play a broad role in the regulation of membrane protein function. The significant changes in the biophysical properties of proteins that are membrane-anchored through GPI in lieu of a hydrophobic transmembrane peptide indicates a variety phobic transmembrane peptide indicates a variety of potential new functions served by the anchor structure itself. Moreover, the number of structural variations within the family of GPI molecules indicates a further opportunity for subspecialization of such anchored proteins, especially regarding cellular localization, mobility, metabolism and susceptibility to enzymatically-induced release. It is likely that further exploration of the structure and function of the GPI anchor may reveal additional roles for this unusual mechanism of membrane-protein attachment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871561
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical characterization of clathrin-associated proteins (CAPs) (1983)
    Springer
    Cell & tissue research 231 (1983), S. 507-518 
    Details
    ISSN: 1432-0878
    Keywords: Clathrin-CAPs complex ; CAPs ; CAPs-subfragments ; Selective absorption ; Immunolocalization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Utilizing antibodies elicited by clathrin-associated proteins (CAPs) absorbed with three different antigenic states of CAPs, i.e., bound to clathrin (clathrin-CAPs complex), free in solution (CAPs) or partially cleaved by chymotrypsin (CAPs-subfragments), indicated that when CAPs are bound to clathrin an antigenic site (or sites) remain(s) unexposed and CAPs-subfragments lose antigenic sites as a result of limited proteolysis. IgG remaining in solution after absorption with CAPs-subfragments were directed against the chymotrypsin-sensitive, or accessible portions of CAPs, whereas IgG remaining after absorption with clathrin-CAPs complex were directed against the unexposed antigenic site(s) characteristic of the clathrin-CAPs complex. Immunocytochemical characterization of these selectively-absorbed IgG solutions suggests that CAPs detected during immunolocalization exist as a complex with clathrin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218109
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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