光谱学与光谱分析
光譜學與光譜分析
광보학여광보분석
SPECTROSCOPY AND SPECTRAL ANALYSIS
2010年
6期
1643-1646
,共4页
邵思蜜%苏海楠%张熙颖%PENG Guo-hong%周百成%张玉忠
邵思蜜%囌海楠%張熙穎%PENG Guo-hong%週百成%張玉忠
소사밀%소해남%장희영%PENG Guo-hong%주백성%장옥충
异藻蓝蛋白%吸收光谱%荧光光谱%圆二色谱%活性构象
異藻藍蛋白%吸收光譜%熒光光譜%圓二色譜%活性構象
이조람단백%흡수광보%형광광보%원이색보%활성구상
Allophycocyanin%Absorption spectra%Fluorescence%Circular dichroism%Active conformation
采用羟基磷灰石层析和离子交换层系的方法从钝顶螺旋藻(Spirulina platensis)分离纯化出异藻蓝蛋白.对异藻蓝蛋白光谱性质受溶液pH变化的影响做了研究.异藻蓝蛋白吸收光谱峰值在650 nm,在620 nm处有1个肩峰,荧光激发光谱的最大发射波长在660 nm.以紫外-可见光吸收光谱表征异藻蓝蛋白对光能的吸收能力,以荧光光谱表征其光能传递能力,以圆二色谱表征其二级结构变化.光谱分析结果表明异藻蓝蛋白在pH为4~10的范围之内,其光能吸收和传递的能力保持在一个相对较稳定的范围内,同时异藻蓝蛋白维持三聚体的形式,而其二级结构则会发生一定程度扰动.在pH值低于4或高于10的范围内,异藻蓝蛋白三聚体发生解聚,二级结构发生剧烈变化,其光能吸收和传递能力迅速被破坏.
採用羥基燐灰石層析和離子交換層繫的方法從鈍頂螺鏇藻(Spirulina platensis)分離純化齣異藻藍蛋白.對異藻藍蛋白光譜性質受溶液pH變化的影響做瞭研究.異藻藍蛋白吸收光譜峰值在650 nm,在620 nm處有1箇肩峰,熒光激髮光譜的最大髮射波長在660 nm.以紫外-可見光吸收光譜錶徵異藻藍蛋白對光能的吸收能力,以熒光光譜錶徵其光能傳遞能力,以圓二色譜錶徵其二級結構變化.光譜分析結果錶明異藻藍蛋白在pH為4~10的範圍之內,其光能吸收和傳遞的能力保持在一箇相對較穩定的範圍內,同時異藻藍蛋白維持三聚體的形式,而其二級結構則會髮生一定程度擾動.在pH值低于4或高于10的範圍內,異藻藍蛋白三聚體髮生解聚,二級結構髮生劇烈變化,其光能吸收和傳遞能力迅速被破壞.
채용간기린회석층석화리자교환층계적방법종둔정라선조(Spirulina platensis)분리순화출이조람단백.대이조람단백광보성질수용액pH변화적영향주료연구.이조람단백흡수광보봉치재650 nm,재620 nm처유1개견봉,형광격발광보적최대발사파장재660 nm.이자외-가견광흡수광보표정이조람단백대광능적흡수능력,이형광광보표정기광능전체능력,이원이색보표정기이급결구변화.광보분석결과표명이조람단백재pH위4~10적범위지내,기광능흡수화전체적능력보지재일개상대교은정적범위내,동시이조람단백유지삼취체적형식,이기이급결구칙회발생일정정도우동.재pH치저우4혹고우10적범위내,이조람단백삼취체발생해취,이급결구발생극렬변화,기광능흡수화전체능력신속피파배.
Allophyeocyanin (APC) was purified from Spirulina platensis using hydroxylapatite chromatogra-phy and ion-exchange chromatography. Effects of solution pH on spectra of APC were studied. APC has an absorption maximum at 650 nm, and a shoulder at 620 nm. The fluorescence emission peak is at 660 nm. The efficiency of energy absorbing and transfer in APC could be reflected by the absorption spectra and fluorescence spectra, respectively. Structural variations of APC could be monitored by means of circular dichroism spectra.APC showed good absorbance and fluorescence stability at varying pH with only minor changes between pH 4-10. The trimeric structure of APC was maintained while local variations of protein peptides were allowed in re-sponse to the environmental disturbance. Beyond this pH range, secondary structure as well as overall confor-mation of APC dramatically changed, and the energy absorption and transfer ability were also disrupted.