A simple,economical method of converting gene expression products of insulin into recombinant insulin and its application  

A simple, economical method of converting gene expression products of insulin into recombinant insulin and its application

在线阅读下载全文

作  者:ZHANG Zhou, CHEN Hui, TANG Yuehua and FENG Youmin(Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China) 

出  处:《Progress in Natural Science:Materials International》2003年第8期596-600,共5页自然科学进展·国际材料(英文版)

基  金:Supported by National "863" Program (863-103-13-01-01)

摘  要:A method, by which the gene expression product of recombinant single chain insulin can be converted into insulin by directly digesting with trypsin, has been established. This method has been used in process of porcine insulin precursor (PIP), [B16Ala] PIP and [B26Ala]PIP into (desB30)insulin, (desB30)[B16Ala]insulin and (desB30)[B26Ala]insulin, respectively, and all of them retain full biological activity of that of their corresponding parent, recombinant human insulin, [B16Ala]insulin and [B26AIa]insulin. The results further demonstrate that the C-terminal residue of B chain is not necessary for insulin's biological activity. Compared with the method of transpeptidation, this method is simple, with a high yield, and avoids the use of organic reagents, and in comparison with the trypsin/carboxypeptidase method, it omits the use of carboxylpeptidase. Besides, (desB30) [B16Ala] insulin and (desB30) [B26AIa]in-sulin still remained without self-association property as that of their parents, which demonstrate that they are monomeric insulin. So they can be used for substituting for monomeric insulin, [B16Ala]insulin and [B26Ala]insulin, in clinical applications.A method, by which the gene expression product of recombinant single chain insulin can be converted into insulin by directly digesting with trypsin, has been established. This method has been used in process of porcine insulin precursor (PIP), [B16Ala]PIP and [B26Ala]PIP into (desB30)insulin, (desB30)[B16Ala]insulin and (desB30)[B26Ala]insulin, respectively, and all of them retain full biological activity of that of their corresponding parent, recombinant human insulin, [B16Ala]insulin and [B26Ala]insulin. The results further demonstrate that the C-terminal residue of B chain is not necessary for insulin's biological activity. Compared with the method of transpeptidation, this method is simple, with a high yield, and avoids the use of organic reagents, and in comparison with the trypsin/carboxypeptidase method, it omits the use of carboxylpeptidase. Besides, (desB30)[B16Ala]insulin and (desB30)[B26Ala]insulin still remained without self-association property as that of their parents, which demonstrate that they are monomeric insulin. So they can be used for substituting for monomeric insulin, [B16Ala]insulin and [B26Ala]insulin, in clinical applications.

关 键 词:INSULIN (desB30)insulin trypsin/carboxylpeptidase transpeptidation monomeric insulin. 

分 类 号:Q786[生物学—分子生物学]

 

参考文献:

正在载入数据...

 

二级参考文献:

正在载入数据...

 

耦合文献:

正在载入数据...

 

引证文献:

正在载入数据...

 

二级引证文献:

正在载入数据...

 

同被引文献:

正在载入数据...

 

相关期刊文献:

正在载入数据...

相关的主题
相关的作者对象
相关的机构对象