水产学报2017，Vol.41Issue(6)：836-844,9.DOI:10.11964/jfc.20160810521
皱纹盘鲍副肌球蛋白的分离纯化及初步性质研究
Isolation and characterization of paramyosin from abalone (Haliotis discus hannai)
摘要
Abstract
In order to investigate the characterization of paramyosin (PM), PM was purified from the muscle of abalone (Haliotis discus hannai) by ammonium sulfate fractionation and hydroxyapatite chromatography. The molecular mass of PM was about 97.0 ku as estimated by SDS-PAGE. Peptide mass fingerprinting of PM obtained 36 peptide fragments with a total of 403 amino acid residues, which were 99.7% and 72.0% identical with PMs from H. discus discus and Crassostres gigas, respectively. The isoelectric point of PM detected by two-dimensional electrophoresis was approximately 5.4, suggesting it is an acidic protein. Circular dichroism spectrum of PM solution demonstrated a rotatory maximum at 192 nm and two negative peaks at 208 nm and 223 nm, indicating the typical spectral characteristic of α-helix structure. Meanwhile, the denaturation temperature (Td) of PM was 58.1 ℃ as determined by circular dichroism spectrum analysis. FTIR spectra further confirmed that PM has intact α-helical structure. The isolation and physicochemical property investigation of PM from the muscle of abalone would provide theoretical foundation for studying proteins related to its texture and for deep-processing of abalone products.关键词
皱纹盘鲍/副肌球蛋白/肽质量指纹图谱/双向电泳/圆二色谱Key words
Haliotis discus hannai/paramyosin/peptide mass fingerprinting/two-dimensional electrophoresis/circular dichroism spectrum分类
轻工纺织引用本文复制引用
游银川,张凌晶,颜龙杰,翁凌,刘光明,曹敏杰..皱纹盘鲍副肌球蛋白的分离纯化及初步性质研究[J].水产学报,2017,41(6):836-844,9.基金项目
国家自然科学基金(31471640) （31471640）
海洋公益性行业专项(201305015) National Natural Scientific Foundation of China (31471640) （201305015）
Public Science and Technology Research Funds Projects of Ocean(201305015) （201305015）
