化工技术与开发
化工技術與開髮
화공기술여개발
TECHNOLOGY & DVELOPMENT OF CHEMICAL INDUSTRY
2014年
4期
15-18
,共4页
王晓霞%张文宁%王正德%刘云颖%闫慧
王曉霞%張文寧%王正德%劉雲穎%閆慧
왕효하%장문저%왕정덕%류운영%염혜
荧光光谱法%牛血清白蛋白(BSA)%铜(Ⅱ)%氯诺昔康%三元配合物
熒光光譜法%牛血清白蛋白(BSA)%銅(Ⅱ)%氯諾昔康%三元配閤物
형광광보법%우혈청백단백(BSA)%동(Ⅱ)%록낙석강%삼원배합물
fluorescence spectroscopy%bovine serum albumin (BSA)%copper (Ⅱ)%lornoxicam%ternary complexes
在生理条件下,用荧光光谱法研究了氯诺昔康对牛血清白蛋白,铜(Ⅱ)对牛血清白蛋白以及铜(Ⅱ)对氯诺昔康和牛血清白蛋白荧光光谱特性的影响。铜(Ⅱ)和氯诺昔康均可使牛血清白蛋白的荧光强度发生猝灭,在铜(Ⅱ)存在下,氯诺昔康对牛血清白蛋白的荧光猝灭作用显著增强。根据荧光猝灭双倒数图计算氯诺昔康和牛血清白蛋白之间的结合常数是5.43×105,结合位点数是1.14。铜(Ⅱ)和牛血清白蛋白之间的结合常数是2.10×105,结合位点数是0.78。
在生理條件下,用熒光光譜法研究瞭氯諾昔康對牛血清白蛋白,銅(Ⅱ)對牛血清白蛋白以及銅(Ⅱ)對氯諾昔康和牛血清白蛋白熒光光譜特性的影響。銅(Ⅱ)和氯諾昔康均可使牛血清白蛋白的熒光彊度髮生猝滅,在銅(Ⅱ)存在下,氯諾昔康對牛血清白蛋白的熒光猝滅作用顯著增彊。根據熒光猝滅雙倒數圖計算氯諾昔康和牛血清白蛋白之間的結閤常數是5.43×105,結閤位點數是1.14。銅(Ⅱ)和牛血清白蛋白之間的結閤常數是2.10×105,結閤位點數是0.78。
재생리조건하,용형광광보법연구료록낙석강대우혈청백단백,동(Ⅱ)대우혈청백단백이급동(Ⅱ)대록낙석강화우혈청백단백형광광보특성적영향。동(Ⅱ)화록낙석강균가사우혈청백단백적형광강도발생졸멸,재동(Ⅱ)존재하,록낙석강대우혈청백단백적형광졸멸작용현저증강。근거형광졸멸쌍도수도계산록낙석강화우혈청백단백지간적결합상수시5.43×105,결합위점수시1.14。동(Ⅱ)화우혈청백단백지간적결합상수시2.10×105,결합위점수시0.78。
Under the physiological conditions, fluorescence spectrometry was used to study bovine serum albumin, copper ( Ⅱ ) of bovine serum albumin and copper ( Ⅱ ) on bovine serum albumin fluorescence spectrum characteristics. Copper ( Ⅱ ) and lornoxicam could both cause bovine serum albumin fluorescence quenched. Under the existence of copper ( Ⅱ ), lornoxicam enhanced the fluorescence quenching effect of bovine serum albumin. According to lineweaver-burk plot calculation, the combining constant between lornoxicam and bovine serum albumin was 5.43×105, position points were 1.14. The combining constant between Copper (Ⅱ) and bovine serum albumin was 2.10×105, position points were 0.78.