Thomas H Lane

Dow Corning Corporation, Seneffe, Walloon Region, United States

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Publications (6)19.86 Total impact

  • Jim Curtis · Thomas H Lane · Warren O Haggard

    No preview · Article · Jan 2008 · The Journal Of Hand Surgery
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    ABSTRACT: A new device for rapid enzymatic debridement of cutaneous wounds has been developed using a controlled-release, silicone-based, dried emulsion. A dehydrated serine protease of the subtilisin family, previously untested for wound debridement, was incorporated into the emulsion. This device exhibited excellent storage stability. Moisture from the wound triggered an even, reproducible, and complete release of the enzyme within the first 8 hours. The device maintains a moist wound environment that allows the enzyme to achieve nearly complete digestion of the hardened eschar of full-thickness burns in a porcine model after an exposure period of 24 hours. Debridement was faster than in untreated wounds or wounds treated with a currently available enzyme ointment. Following rapid enzymatic debridement, healing appeared to progress normally, with no histological evidence of damage to adjacent healthy tissue.
    No preview · Article · Mar 2007 · Wound Repair and Regeneration
  • Thomas H Lane
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    ABSTRACT: The paper by Lykissa and Maharaj (Lykissa, E. D.; Maharaj, S. V. M Anal. Chem. 2006, 78, 2925-2933) purports to provide evidence that the urine of women with silicone breast implants contain 60 to over 1700 times more platinum in their urine that the urine of people with no known exposure to platinum. Further, they purport to show evidence that the platinum used in the manufacture of breast implants (Pt0) is converted by a unknown process to yield highly oxidized platinum species, stable in biological matrixes, up to and including Pt6+. This correspondence poses three questions associated with the work and directs the reader's attention to the data, which clearly show that the blood and urine platinum levels in implanted women and their healthy control group were not significantly different from one another.
    No preview · Article · Sep 2006 · Analytical Chemistry
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    ABSTRACT: Immobilized lipase B from Candida antarctica (Novozyme 435) catalyzed the regioselective formation of ester bonds between organosilicon carboxylic diacids and a C1-O-alkylated sugar under mild reaction conditions (i.e., low temperature, neutral pH, solventless). Specifically, the acid-functionalized organosilicones reacted with the primary hydroxyl group at the C6 position of alpha,beta-ethyl glucoside during the regioselective esterification. The pure organosilicon-sugar conjugates were prepared in a one-step reaction without protection-deprotection steps and without activation of the acid groups with the integrity of the siloxane bonds. [reaction: see text]
    No preview · Article · Oct 2005 · Organic Letters
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    ABSTRACT: The intricate siliceous architectures of diatom species have inspired our exploration of biosilicification. In order to better understand the role of various proteins in the biosilicification process, a carefully chosen model study was performed to test the ability of homologous enzymes to catalyze the formation of molecules with a single siloxane bond during the in vitro hydrolysis and condensation of alkoxysilanes. This model study is believed to be the first rigorous study to demonstrate biocatalysis at silicon. Our data suggests that homologous lipase and protease enzymes catalyze the formation of siloxane bonds under mild conditions. In particular, the active site of trypsin, a proteolytic enzyme, was determined to selectively catalyze the in vitro condensation of silanols. Conversely, the reverse reaction was not favored. Furthermore, trypsin as well as several other proteins and polypeptides promoted the hydrolysis of alkoxysilanes in a non-specific manner. Given the selectivity and mild reaction conditions of enzymes, the opportunity to strategically use biocatalysts to synthesize novel hybrid materials with structural control and spatial order is promising.
    No preview · Article · Feb 2005 · ACS Symposium Series
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    ABSTRACT: Biosilicification occurs on a globally vast scale under mild conditions. Although research has progressed in the area of silica biosynthesis, the molecular mechanisms of these interactions are effectively unknown. The natural production of silica in the Tethya aurantia marine sponge, Cylindrotheca fusiformis diatom, and Equisetum telmateia plant appear to be similar. However, the studies were complicated mechanistic queries due to the use of silicic acid analogues. Given these complications, a carefully chosen model study was carried out to test the ability of enzymes to catalyse the formation of molecules with a single siloxane bond during the in vitro hydrolysis and condensation of alkoxysilanes. Our data suggest that homologous lipase and protease enzymes catalyse the formation of siloxane bonds under mild conditions. Non-specific interactions with trypsin promoted the in vitro hydrolysis of alkoxysilanes, while the active site was determined to selectively catalyse the condensation of silanols.
    No preview · Article · Sep 2003 · Journal of Inorganic Biochemistry