CAJ | 학술논문

利用FPLC技术从萱草花粉中鉴定并纯化了动力蛋白,研究了它的酶学性质及部分生物化学性质.结果如下:纯化的类动力蛋白分子量为100 kD,等电点pI=6.15和6.80.在280 nm波长激发下,最大的荧光发射波长是346 nm.荧光光谱分析结合紫外吸收光谱及导数光谱分析推断它含有色氨酸和酪氨酸残基.药理学性质研究表明巯基可能在酶的活性中心起重要作用.
이용FPLC기술종훤초화분중감정병순화료동력단백,연구료타적매학성질급부분생물화학성질.결과여하:순화적류동력단백분자량위100 kD,등전점pI=6.15화6.80.재280 nm파장격발하,최대적형광발사파장시346 nm.형광광보분석결합자외흡수광보급도수광보분석추단타함유색안산화락안산잔기.약이학성질연구표명구기가능재매적활성중심기중요작용.
A novel motor protein, dynamin-like protein from day lily, was purified and identified by FPLC. Here we report its biochemical characterization. The molecular weight of the dynamin-like protein is 100 kD on SDS-PAGE. Isoelectric points are about 6.15 and 6.80. The fluorescence emission wave length of dynamin-like protein is 346 nm by excitation at 280 nm. Through fluorescence spectra analysis, ultraviolet absorption spectrum and derivative spectrum, we conclude that it contains tryptophan and tyrosine residues. Pharmacological study indicates that mercapto may play an important role in enzyme activity of dynamin-like protein.