Today's Hours: 10:00am - 6:00pm
Lane Medical Library

Search

Filter Results

Did You Mean:

Search Results

Sort by
relevance
  • Book
    Jorge Perdigão.
    Contents:
    1. Endodontic considerations for the restoration of endodontically treated teeth --2. Effect of endodontic treatment procedures on canal shape and mechanical properties of a tooth
    3. Restoring the endodontically treated tooth: treatment planning considerations
    4. Fiber-reinforced dental materials in the restoration of root-canal treated teeth
    5. Biomechanical principles of root canal-treated-teeth restored with fiber-reinforced resin posts
    6. Fiber-reinforced resin posts (fiber posts)
    7. Adhesion to root dentin: a challenging task
    8. Methods for increasing the longevity of adhesion to root canal dentin
    9. Selection of luting materials for bonding fiber posts
    10. Provisional restorations
    11. Cast dowel and core
    12. Clinical sequence.
    Digital Access Springer 2016
  • Article
    Bonomi F, Pagani S, Cerletti P, Cannella C.
    Eur J Biochem. 1977 Jan 03;72(1):17-24.
    The interaction of the sulfurtransferase rhodanese (EC 2.8.1.1) with succinate dehydrogenase (EC 1.3.99.1), yeast alcohol dehydrogenase (EC 1.1.1.1) and bovine serum albumin was studied. Succinate dehydrogenase incorporates the sulfane sulfur of [35S]rhodanese and, in the presence of unlabelled rhodanese, also incorporates that of [35S]thiosulfate. Rhodanese releases most of its transferable sulfur and is re-loaded in the presence of thiosulfate. Rhodanese undergoes similar modifications with yeast alcohol dehydrogenase but this latter does not bind 35S in amounts comparable to those incorporated in succinate dehydrogenase: nearly all the 35S released by [35S]rhodanese is with low-molecular-weight compounds. Bovine serum albumin also binds very little sulfur and [35S]rhodanese present in the reaction mixture does not discharge its radioactive sulfur nor does it take up sulfur from thiosulfate. Sulfur release from rhodanese appears to depend on the presence of - SH groups in the acceptor protein. Sulfur incorporated into succinate dehydrogenase was analytically determined as sulfide. A comparison of the optical spectra of succinate dehydrogenase preparations incubated with or without rhodanese indicates that there is an effect of the sulfurtransferase on the iron-sulfur absorption of the flavorprotein. The interaction of rhodanese with succinate dehydrogenase greatly decreases the catalytic activity of rhodanese with respect to thiocyanate formation. This is attributed to modifications in rhodanese associated with the reduction of sulfane sulfur to sulfide. Thiosulfate in part protects from this deactivation. The reconstitutive capacity of succinate dehydrogenase increased in parallel with sulfur incorporated in that enzyme following its interaction with rhodanese.
    Digital Access Access Options