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
    Multiple denaturational transitions in fibrillar collagen (1986)
    New York : Wiley-Blackwell
    Biopolymers 25 (1986), S. 1875-1893 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The heat denaturation of pepsinized bovine nonfibrillar and fibrillar collagen was studied by differential scanning calorimetry. For fibrillar preparations that had been rapidly precipitated with stirring at low ionic strength, then resuspended at physiological ionic strength, multiple denaturational transitions were observed. At heating rates of 10°C/min, melting endotherms occurred at about 44, 50, 53, and 57°C. Fibrillar collagen that was slowly gelled without stirring at physiological ionic strength exhibited a similar series of endotherms, but the lower melting transitions were less conspicuous. In contrast, nonfibrillar bovine collagen in acidic solution showed only a single denaturational transition at 40°C. Nonfibrillar solutions at pH 7, to which inhibitors of fibrillogenesis were added, showed a major endotherm as high as 46°C. These results suggest that reconstituted fibrillar collagen contains a heterogeneous fibril population, possibly including molecules in a nonfibrillar state. It was proposed that the multiple melting endotherms of such preparations were due to sequential melting of molecular and fibril classes, each with a distinct melting temperature. The fibrillar classes may represent three or more types of banded and nonbanded species that differ from each other in packing order, collagen concentration, and possibly also in fibril width and level of cross-linking.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360251006
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    A comparative study of the biologic and immunologic response to medical devices derived from dermal collagen (1986)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 20 (1986), S. 109-120 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: We examined collagen materials for soft tissue augmentation [Zyderm® Collagen Implant (ZCI), glutaraldehyde cross-linked (GAX) collagen, and Koken Atelocollagen (Atelocollagen)]; hemostatic collagens [Gelfoam® Gelatin Powder (Gelfoam), Avitene® Microfibrillar Collagen Hemostat (Avitene), and Collastat® Collagen Hemostat (Collastat)]; and reconstituted, intact fibrillar collagen from bovine skin in a subcutaneous guinea pig model. After 11, 25, and 39 days in situ, explants from animals injected with GAX collagen demonstrated greater wet-weight persistence than all other materials. Conversely, at all time points, the explants of Atelocollagen were the least persistent. Following 25 days in vivo, explants were examined using differential scanning calorimetry; ZCI and Atelocollagen displayed thermal transition temperatures of 58°C. Avitene and Gelfoam explants displayed transition points of 30°C and 32°C, indicating denatured or cleaved collagen. By contrast, GAX collagen explants had a high (68°C) transition temperature, reflecting its cross-linking. With respect to immunogenicity, day 39 sera from ZCI treated animals showed significantly lower titers in the ELISA to their respective implant collagen than all other groups examined, while antibody activity in the GAX collagen, Gelfoam, Atelocollagen, and intact collagen groups were not significantly different. Collastat elicited antibodies with a greater affinity than observed in these previous groups. Sera from Avitene treated animals demonstrated the highest antibody levels and were the only sera which reacted with bovine serum albumin. Thus, Avitene was the most immunogenic of the collagen materials examined, while GAX collagen demonstrated the greatest persistence and minimal immunogenicity, and ZCI was the least immunogenic.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820200110
    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...