中华鲟软骨Ⅱ型胶原蛋白的结构分析

车帅; 杜芬; 刘楚怡; 李八方

中华鲟软骨Ⅱ型胶原蛋白的结构分析

The structure analysis of type Ⅱ collagen from sturgeon(Acipenser sinensis)cartilage

摘要

摘要: 采用胃蛋白酶辅助提取的方法提取了中华鲟鱼软骨中Ⅱ型胶原蛋白(Pepsin soluble collagens,PSCⅡ),并对其组成与结构进行了分析。结果显示,PSCⅡ在约110 kDa附近有单一的α1亚基,在200 kDa左右有一条二聚体β亚基。在229 nm出现最大紫外吸收峰,傅里叶变换红外光谱分析与圆二色谱结果均符合Ⅱ型胶原蛋白的特征。氨基酸分析表明PSCⅡ中甘氨酸的含量最高,约占总氨基酸残基数的1/3,富含丙氨酸和脯氨酸残基。热稳定分析表明,PSCⅡ热变性温度为31.5 ℃。扫描电镜显示PSCⅡ为不规则多孔状结构,可以作为良好的药物载体。

Abstract: In this paper,the pepsin soluble type Ⅱ collagen(PSCⅡ)was extracted by pepsin from sturgeon(Acipenser sinensis)cartilage and its structure was characterized. The SDS-PAGE result showed that the PSCⅡ possessed two kinds of chains(α1 and β)and the molecular weight was about 110 and 200 ku,respectively. The maximum UV absorption of PSCⅡ was 229 nm and the fourier transform infrared(FTIR)and circular dichrosim(CD)results accorded with the characteristics of type Ⅱ collagen form other species. The amino acid analysis showed glycine was the highest population in PSCⅡ with the ratio of 1/3. Meanwhile,PSCⅡ was rich in alanine and proline. Differential scanning calorimeter(DSC)results showed the thermal denaturation temperature of PSCⅡ was 31.5 ℃. PSCⅡ could be used as a good drug carrier because of its porous structure under scanning electron microscope(SEM).