黄粉虫纤溶活性蛋白酶(TFP)酶学性质以及红外光谱分析  

Infrared Spectral Analysis and Enzymological Characteristic of Tenebrio Fibrinolyric Proteins(TFP)

作　　者：吴艳玲[1] 谭竹钧[1] 韩雅莉[1] 林非凡[1] 陈雅雄[1] 余磊[1] 汪威[1] 张丽[1] 

机构地区：[1]广东工业大学轻工化工学院,广东广州510006

出　　处：《时珍国医国药》2011年第9期2061-2064,共4页Lishizhen Medicine and Materia Medica Research

基　　金：国家自然科学基金(No.30772739);广东工业大学轻工化工学院"211工程"培育项目(No.20091015)

摘　　要：目的研究黄粉虫纤溶活性蛋白(Tenebrio Fibrinolyric Proteins,TFP)的酶学性质及对其进行分类。方法以BAEE、BAPNA和酪蛋白为底物分别测TFP的Km值;分别研究PMSF和胰蛋白酶对TFP活性的影响。结果以BAEE和BAPNA为TFP底物,Km值分别为0.182 mmol/L和1.138 mmol/L,表明TFP与BAEE亲和力最好,酯酶活力>酰胺酶活力>肽键酶活力。丝氨酸蛋白酶抑制剂PMSF能有效抑制TFP活性,而偏弱碱性环境下胰蛋白酶未降解TFP,胰蛋白酶与TFP红外结构图谱相似,可以初步证明TFP属于丝氨酸蛋白酶。结论黄粉虫纤溶活性蛋白酶的酯酶活力最好,属于丝氨酸蛋白酶。Objective To study enzymological characteristic of Tenebrio Fibrinolyric Proteins（TFP） and to determine its enzymological classification. Methods The Km of TFP was detected by using BAEE,BAPNA and the casein as substrate,and the effects of PMSF and trypsin on fibrinolytic activity of TFP were studied. Results The Km of TFP were 0.182 mmol/L and 1.138 mmol/L detected separately by using BAEE and BAPNA as substrate,and it showed that TFP had the strongest affinity to BAEE-esterase activityActivity of non-peptide bond amidePeptidase activity.The fibrinolytic activity of TFP could be inhibited effectively by PMSF,the inhibitor of serine proteinase.While TFP wasn＇t decomposed by the trypsin in the simulation of the leaning weak basicity.The infrared chart demonstrated that trypsin and TFP had similar structure,so the synthesis above might prove initially that TFP belonged to the serine proteinase as same as the trypsin. Conclusion TFP has the best esterase activity and the strongest affinity with BAEE,and it belongs to the serine proteinase.

关 键 词：黄粉虫纤溶活性蛋白 KM 丝氨酸蛋白酶 胰蛋白酶 红外光谱 

分 类 号：O629[理学—有机化学]