Band3蛋白关联的一种新活性蛋白酶的纯化、基因克隆及其特性研究

The peptide C1(Ala893-Val911) of band 3 C-terminal domain was purified from the human erythrocyte membrane in our former research work and discovered that the C1 peptides can activate a novel protease which cleaved glycophorin A(GPA) at Leu118~Ser119.According to this result,we designed a precept to purify the protease and clone the gene of it.Whereas,the further research showed that there is a direct interaction relationship between erythrocyte band 3 C-terminal domain and C-terminus of GPA,this means that the band 3 C-terminus prosess protease activity above.Since we prossessed the full length gene of band 3,our later research work focused on the biologic properties of band 3 C-terminus.Using band 3 C-terminus as a bait, the proteins which interact with band 3 c-terminus were screened from K562 cDNA library.DNA sequence analysis and the Genebank homology analysis revealed that the cDNA from the positive clones were fragments of tumer suppressor gene p16 INK4 (cyclin-dependent kinase inhibitor).Based on the results above,we concluded that band 3 not only interact with GPA,but also has the binding site of p16.The interaction of band 3 C-terminus and p16 INK4 was confirmed and might directly affect the growth and apoptosis of the cells. This innovative theory is significant for the further research work..

本课题是关于一种新活性蛋白酶纯化、克隆及其特性的研究。.课题申请人在过去几年关于Band3蛋白C末端的研究中发现了一种.能被Band3特异激活，然后特异地水解红细吞堑鞍譇L118-S.119结合键，到目前为止尚没有发现关于此酶的任何报道。这项研究峁馐秃煜赴纳硐窒筇峁┬碌囊谰荩⒔哉庖涣?.域的研究趋势产生重大影响