CAJ | 학술논문

为研究 60Coγ射线辐照剂量对牛血清蛋白结构的影响,以单一组分牛血清白蛋白(BSA)为模型,研究BSA水溶液辐照0~50 kGy剂量后的含量、结构和微观形态变化. 结果表明,BSA主要由25~214 kDa约10种分子量的蛋白质组成,其中55 kDa的蛋白质含量最大,各组分含量随辐照剂量的增加而下降,辐照50 kGy时几乎全部降解;BSA在210、280 nm处各有1个紫外吸收峰,峰高均随着剂量的增加而下降,辐照30 kGy时280 nm处的峰消失;BSA二级结构中α-螺旋、β-折叠和β-转角、无规卷曲含量分别为40.8%、37.3%和21.9%,α-螺旋含量随辐照剂量增加而下降,其他结构含量呈上升趋势;辐照前后BSA的酰胺I带红外吸收峰从1 650.8 cm-1红移至1 655.5 cm-1处;BSA辐照后微观表面由平滑变为褶皱, 形成松散的片状. 辐照后牛血清白蛋白二级结构发生变化,辐照剂量越大,反应程度越大.
위연구 60Coγ사선복조제량대우혈청단백결구적영향,이단일조분우혈청백단백(BSA)위모형,연구BSA수용액복조0~50 kGy제량후적함량、 결구화미관형태변화. 결과표명,BSA주요유25~214 kDa약10충분자량적단백질조성,기중55 kDa적단백질함량최대,각조분함량수복조제량적증가이하강,복조50 kGy시궤호전부강해;BSA재210、280 nm처각유1개자외흡수봉,봉고균수착제량적증가이하강,복조30 kGy시280 nm처적봉소실;BSA이급결구중α-라선、β-절첩화β-전각、 무규권곡함량분별위40.8%、37.3%화21.9%,α-라선함량수복조제량증가이하강,기타결구함량정상승추세;복조전후BSA적선알I대홍외흡수봉종1 650.8 cm-1홍이지1 655.5 cm-1처;BSA복조후미관표면유평활변위습추, 형성송산적편상. 복조후우혈청백단백이급결구발생변화,복조제량월대,반응정도월대.
To study the influence of 60Co γ ray irradiation dose on bovine serum component,as a single component model,BSA solution was irradiated by 0~50 kGy respectively and the protein content,secondary structure molecular and morphology were determined. The results showed that the BSA was mainly composed of 10 proteins and the molecular weights were 25~214 kDa,of which the protein content of 55 kDa was the largest one. The protein content was decreased with the increasing of irradiation dose and the content of 10 proteins were degraded after irradiated 50 kGy. The UV-Vis (UV -Visible Spectrophotometer) of BSA appeared two absorption peaks at 210 nm and 280 nm,respectively. The height of two peaks were decreased with the dose increasing and 1 280 nm-peak disappeared after the BSA was irradiated by 30 kGy. The secondary structure content of α-helix,β-fold & β-corner and random coil from BSA were 40.8%,37.3% and 21.9%. The α-helix content decreased with the dose increasing and the other structural content increased with the dose increading. Amide I band of infrared absorption peak of bovine serum albumin shifted from 1 650.8 cm-1 to 1 655.5 cm-1. The BSA had a smooth surface microstructure before irradiation and changed into a loose sheet after irradiaton. Thus,the main effect region of the radical irradiation was α-helix of BSA,subsequently led the increasing of β-fold,β-turn and random coil increases,finally the protein turned from the ordered state into a disordered state,the greater the dose,the greater the degree of reaction.