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Allergenicity Test of Genetically Modified Soybean in Sprague Dawley Rats
Chang, Hyun Sung,Bae, Youn Kyoung,Lim, Si Kyu,Jeong, Tae Cheon,Kim, Hyung Soo,Chung, Seung Tae,Kim, Dong Sup,Nam, Doo Hyun 영남대학교 약품개발연구소 2001 영남대학교 약품개발연구소 연구업적집 Vol.11 No.-
Allergenicity of genetically-modified (GM) soybean was evaluated in male Sprague Dawley rats. To confirm the GM soybean used in this study, the polymerase chain reaction (PCR) was performed using the chromosomal DNA of soybeans. The PCR result provided the clear discrimination of genetically-modified (GM) soybeans. To evaluate the allergenicity of GM soybean and non-GM control one, the soybean homogenate was sensitized subcutaneously 3 times a week for 3 weeks. The doses of soybean were 0, 2 and 20 mg/kg of soybean homogenate containing 1% Evans blue, no sign of passive cutaneous anaphylaxis reaction was detected. In addition, when the sera were treated in the cultures of peritoneal mast cells, the increase of histamine release by anti-(GM soybean) sera was not observed when compared to that by anti-(non-GM soybean) sera. The present results indicate that the GM soybean might not act as a strong allergen in male Sprague Dawley rats.
Thioacetamide에 의한 BALB/c 마우스 간의 시간별 약물대사효소 억제 양상 : A Time-Course Study
이정운,고우석,김갑호,배연경,하현정,한상섭,천영진,정태천 영남대학교 약품개발연구소 2001 영남대학교 약품개발연구소 연구업적집 Vol.11 No.-
Thioacetamide is a potent hepatotoxicant which requires metabolic activation by cytochrome P450s (P450s) for toxicity. In the present study, the elevation kinetic of serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) activities by thioacetamide treatment was investigated in male BALB/c mice. Inaddition, the inhibitory effects of thioacetamide on liver microsomal P450 enzymes were further investigated. Thioacetamide at 100 mg/kg/ was treated intraperitoneally for 6, 12, 24, 36, 48 and 72 hr. The blood was collected at the designated time for assaying the serum enzyme activities. To determine the P450 isozyme-specific activities. ethoxyresorufin O-deethylase (EROD), methoxyresorufin O-demethylase (MROD), and benzyloxyresorufin O-debenzylase (BROD) activities were determined for P450 1A1, 1A2 and 2B1, respectively, in liver microsomal fractions. The activities of ALT and AST were started to be elevated 6 hr after thioacetamide treatment andreached the maximun at 36 hr after the treatment. The elevated activities were dramatically recovered at 72 hr. The microscopic exmination of the liver specimen also showed a similar profile of hepatotoxicity. All P450-associated enzyme activities were time-dependently inhibited by the treatiment with thioacetamide. The maximum inhibition of P450 enzymes was observed 36 hr after the treatment. Because the inhibition of P450 enzymes by thioacetamide was time-dependent, our present results suggest that thioacetamide might inhibit P450 enzymes in mechanism-based inactivation.