摘要
作者在对背角无齿蚌外套膜中分离提纯到的一种酸性磷酸酶 (ACPase)的部分酶学性质进行研究的基础上 ,测定了该酶的亚基分子量为 6 1,80 0D ,等电点 (pI)为 6 .12 (2 5℃ ) ,并对其氨基酸组成进行了分析 .对ACPase的二级结构的圆二色谱 (CD)分析显示 ,酶分子中α 螺旋占 31.8% ,β 折叠占 4 2 .6 % ,β 转角 17.9% .对ACPase进行了化学修饰研究 ,初步认为组氨酸、丝氨酸、色氨酸和半胱氨酸有可能是该酶的功能基团 ,二硫键也对维持酶的活性中心构象极为重要 .
On the fo undation of previous work, the authors have studied some properties of acid phosphatase (ACPase, E.C.3.1.3.2 ) that was purified from the mantle of Anodonta woodiana (Heude) .Its subunit is 61 800 D as determined with SDS PAGE and its pI is 6.12 (25℃).The authors have alsoanalysised the compose of amino acid of ACPase. It has been demonstrated that the enzyme has 31.8% α helix, 42.6% β pleated, 17.9% β turn by the analysis of CD. His, Ser, Trp and Cys are demonstrated to be essential functional groups of the enzyme by chemical modification. The disulfide bond is very important in keeping the conformation of the active center of enzyme.
出处
《四川大学学报（自然科学版）》
CAS
CSCD
北大核心
2002年第1期111-114,共4页
Journal of Sichuan University(Natural Science Edition)
基金
国家自然科学基金 (39770 5 86 )
