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Chemical modification of L-asparaginase with N, O-carboxymethyl chitosan and its effects on plasma half-life and other properties
作者姓名:钱国强  周菊岩  马建标  何炳林  王道宾
作者单位:Institute of Polymer Chemistry,Nankai University,Tianjin 300071,China,Institute of Polymer Chemistry,Nankai University,Tianjin 300071,China,Institute of Polymer Chemistry,Nankai University,Tianjin 300071,China,Institute of Polymer Chemistry,Nankai University,Tianjin 300071,China,Institute of Polymer Chemistry,Nankai University,Tianjin 300071,China
基金项目:Project supported by the National Natural Science Foundation of China,the 21st Century Foundation for Young Scholars of Tianjin
摘    要:E.coli L-asparaginase,an antitumor enzyme,was chemically modified with N,O-carboxymethyl chitosan to lower its artigenicity and increase its plasma half-life.The results showed that the modified L-asparaginase has almost the same apparent Km value as that of native enzyme.The modified L-asparaginase also showed a higher protease stability against trypsin and a-chymotrypsin.After being modified,the enzyme exhibited the complete loss of antigenicity towards antiasparaginase serum.In addition,the higher the molecular weight of modifying reagents,the better the effects on reduction of antigenicity.When tested in vivo,the plasma half-life of the modified enzyme (t1/2=40 h) was over 33 times longer than that of the native enzyme (t1/2=1.2 h).

收稿时间:2 August 1996

Chemical modification of L-asparaginase with N, O-carboxymethyl chitosan and its effects on plasma half-life and other properties
Guoqiang Qian,Juyan Zhou,Jianbiao Ma,Binglin He,Daobin Wang.Chemical modification of L-asparaginase with N, O-carboxymethyl chitosan and its effects on plasma half-life and other properties[J].Science in China(Chemistry),1997,40(4):337-341.
Authors:Guoqiang Qian  Juyan Zhou  Jianbiao Ma  Binglin He  Daobin Wang
Institution:(1) Institute of Polymer Chemistry, Nankai University, 300071 Tianjin, China
Abstract:E.coli L-asparaginase,an antitumor enzyme,was chemically modified with N,O-carboxymethyl chitosan to lower its artigenicity and increase its plasma half-life.The results showed that the modified L-asparaginase has almost the same apparent Km value as that of native enzyme.The modified L-asparaginase also showed a higher protease stability against trypsin and a-chymotrypsin.After being modified,the enzyme exhibited the complete loss of antigenicity towards antiasparaginase serum.In addition,the higher the molecular weight of modifying reagents,the better the effects on reduction of antigenicity.When tested in vivo,the plasma half-life of the modified enzyme (t1/2=40 h) was over 33 times longer than that of the native enzyme (t1/2=1.2 h).
Keywords:N  O-carboxymethyl chitosan  L-asparaginase  chemical modification
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