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  • 2-hydroxypropyl-β-cyclodextrin  (1)
  • 25 Jahre später  (1)
  • Cell & Developmental Biology  (1)
  • 1
    German Medical Science GMS Publishing House; Düsseldorf
    In:  46. Jahrestagung der Deutschen Gesellschaft der Plastischen, Rekonstruktiven und Ästhetischen Chirurgen (DGPRÄC), 20. Jahrestagung der Vereinigung der Deutschen Ästhetisch-Plastischen Chirurgen (VDÄPC); 20151001-20151003; Berlin; DOC251 /20150928/
    Publication Date: 2015-09-29
    Keywords: Rezidiv ; Morbus Paget ; 25 Jahre später ; Nipple Sharing Technik ; ddc: 610
    Language: German
    Type: conferenceObject
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  • 2
    ISSN: 0886-1544
    Keywords: motility ; flagellum ; spermatozoon ; nexin ; freeze-etch ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this work, we examine whether the “nexin” linkages of the flagellum can extend in length to accommodate interdoublet sliding. Flagellar bends of large angle were induced in bull spermatozoa by hypotonic treatment. It is argued that this produces large interdoublet displacements that are, nevertheless, still within physiological limits. Such flagella were examined by the rapid-freeze, deep-etch techique and the nexin linkages identified by their position in relation to the inner dynein arms and by their straplike, bipartite, morphology. They were found to bridge perpendicularly (or occasionally at an angle) between the A- and B-tubules of adjacent doublets. The nexin linkages were no more than ∼20 nm in length, even in regions in which ∼200 nm of sliding could be inferred. Variable registration between adjacent nexin rows gave some further support to the assumption that sliding had indeed taken place. From this, it is concluded that elastic deformation of the links, such as would accommodate interdoublet sliding, does not occur; some form of displacement must occur between nexin and the adjacent B-tubule. © 1993 Wiley-Liss, Inc.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-1111
    Keywords: Inclusion complexation of warfarin withβ-CDs ; apparent binding constants ; bioavailability of warfarin ; β-CD complexes ; fluorescence spectroscopy ; β-cyclodextrin ; 2-hydroxypropyl-β-cyclodextrin ; methyl-β-cyclodextrin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The inclusion complexes of warfarin withβ-cyclodextrin, 2-hydroxypropyl-β-CD and methyl-β-CD have been investigated in aqueous solution. The apparent binding constants of warfarin are found to be 542±19, 442±18 and 112±6M−1 respectively, calculated from the increments in fluorescence emission of the drug. The influence of theβ-CDs on the absorption rate of the drug is investigated within situ experiments in a chronically isolated internal loop, in the small intestine of the rat. The first-order disappearance (absorption) rate constant decreases to 3.6×10−4 min−1 inβ-CD, to 5.0×10−4 min−1 in 2-hydroxypropyl-β-CD and to 1.4×10−3 min−1 in methyl-β-CD compared to 3.2×10−3 min−1 in isotonic phosphate buffer (pH=7.4) solution, all of them showing a good agreement with the percentage of free warfarin in their complexed solutions: 16%, 18% and 47% calculated, respectively.
    Type of Medium: Electronic Resource
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