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1.
J Biomater Sci Polym Ed ; 8(10): 779-95, 1997.
Artigo em Inglês | MEDLINE | ID: mdl-9297603

RESUMO

Although biodegradation of model poly(ester-urethane)s and poly(ether-urethane)s has been demonstrated using a single enzyme system (cholesterol esterase (CE) in vitro, in vivo biodegradation most likely involves many processes acting together. In this study, the physical (film vs textured surface) and chemical (poly(urethane)s containing polycaprolactone (PCL) vs poly(tetramethylene oxide) (PTMO)) nature of the materials as well as the products of enzymatic reactions known to occur during the inflammatory response (CE and phospholipase A2 (PLA)) were assessed for their effects on poly(urethane) (PU) biodegradation in vitro. A mixed micelle (phosphatidylcholine (PC):lysoPC (LPC):oleic acid (OA): 2:1:1) significantly increased the release of radiolabelled products from a C-labelled poly(ester-urethane) (TDI/PCL/ED) caused by CE. This effect was further enhanced when this material was cast as a textured surface. A model poly(ether-urethane) showed no significant enhancement of CE-mediated hydrolysis in the presence of phospholipids and their breakdown products whether cast as a film or a textured surface. PLA caused a small but significant release of radiolabel from TDI/PCL/ED which was enhanced in the presence of its substrate, PC, and a mixture of PC with its breakdown products, LPC and OA. Based on the results of this study, it may be possible to hypothesize that during the inflammatory response when PLA is activated, enhancement of the biodegradation of a PU could occur by direct action of PLA on the poly(ester-urethane) and by stimulation of CE due to the formation of LPC and OA occurring when PLA hydrolyses PC, its natural substrate


Assuntos
Materiais Biocompatíveis/metabolismo , Glicóis/metabolismo , Fosfolipases A/toxicidade , Poliésteres/metabolismo , Poliuretanos/metabolismo , Esterol Esterase/toxicidade , Materiais Biocompatíveis/química , Biodegradação Ambiental , Radioisótopos de Carbono , Ativação Enzimática , Glicóis/química , Marcação por Isótopo , Lisofosfatidilcolinas/química , Lisofosfatidilcolinas/metabolismo , Micelas , Microscopia Eletrônica de Varredura , Ácido Oleico/química , Ácido Oleico/metabolismo , Fosfatidilcolinas/química , Fosfatidilcolinas/metabolismo , Fosfolipases A2 , Poliésteres/química , Propriedades de Superfície , Fatores de Tempo
2.
Biochem Biophys Res Commun ; 196(3): 1406-13, 1993 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-8250897

RESUMO

The discovery of proteins that control insects is critical for the continued growth of the agricultural biotechnology industry. A highly efficacious protein that killed boll weevil (Anthonomus grandis grandis Boheman) larvae was discovered in Streptomyces culture filtrates. The protein was identified as cholesterol oxidase (E.C. 1.1.3.6). Purified cholesterol oxidase was active against boll weevil larvae at a concentration (LC50 = 20.9 micrograms/ml) comparable to the bioactivity of Bacillus thuringiensis proteins against other insect pests. Histological studies demonstrated that cholesterol oxidase lysed the boll weevil midgut epithelium, suggesting that this is the primary mechanism of lethality.


Assuntos
Proteínas de Bactérias/toxicidade , Besouros/efeitos dos fármacos , Inseticidas/toxicidade , Esterol Esterase/toxicidade , Streptomyces/enzimologia , Sequência de Aminoácidos , Animais , Bacillus thuringiensis , Dieta , Gossypium , Larva , Dados de Sequência Molecular , Homologia de Sequência de Aminoácidos
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