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�й����ﻯѧ���������ѧ�� 2005, Vol. 21 Issue (05 ):603-603     DOI:
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ZHU Xue-Wei, WU Gang, ZENG Wu-Wei, XUE Hong, CHEN Bao-Sheng *(National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100005, China)

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ժҪ Ϊ̽������֬����A-��(apoA-��,apolipoproteinA-��)������ͬλ��İ��װ���ͻ���,�Ե��׶����ṹ��֬�ʽ��������Ӱ��,���ö����ձ似������apoA-�����Ȼ���װ���ͻ����apoA-��Milano(R173C),�����������Ƭ���ϵİ��װ���ͻ����,�ֱ�ΪapoA-��(S52C),apoA-��(N74C),apoA-��(L107C),apoA-��(K129C),��apoA-��(L195C).�۲�Ƚϸ���Ұ���ͼ�ͻ��apoA-���嵰�׵Ħ��������Ͷ����ṹ�ȶ��Լ���֬�ʽ������.�����ʾ,Ұ����apoA-��,apoA-��(S52C),apoA-��(N74C),apoA-��(L107C),apoA-��(K129C),apoA-��Milano��apoA-��(L195C)�Ħ��������ֱ�Ϊ54��4%,49��4%,50��2%,51��6%,56��4%,52��3%,��54��1%,���ֵ��׵Ħ��������������Բ���(P>0.05).Ұ����apoA-��ı��Ա�׼������(��G0D)Ϊ10.5kJ/mol;apoA-��(S52C)��apoA-��Milano�Ħ�G0D��Ұ���͵�2.1kJ/mol;��apoA-��(K129C)�Ħ�G0D��Ұ����apoA-���1.6kJ/mol.��Ұ����apoA-�����,apoA-��(K129C)��apoA-��(L195C)����ͻ������֬�ʽ�����������½�(P<0.05),��������װ���ͻ����(����apoA-��Milano)��֬�ʽ�϶���ѧ������Ұ����apoA-�������Բ���.���Ͻ����ʾ,��ͬλ�㷢��İ��װ���ͻ���apoA-���嵰�׵Ħ�������������Ӱ��,���Ե��׵Ķ����ṹ�ȶ��Ժ�֬�ʽ������Ӱ�첻����ͬ.
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Abstract�� To explore the influences of cysteine mutations at the different sites of helices upon the secondary structural and functional properties of human apolipoprotein A-��(apoA-��),site-directed mutagenesis was employed to construct the natural (apoA-��_ Milano , R173C) or unnatural cysteine mutants of apoA-��, named as apoA-�� (S52C), apoA-��(N74C), apoA-��(L107C), apoA-��(K129C), and apoA-��(L195C), respectively. For the recombinant proteins, the �� helical contents, the secondary structural stability and the capabilities to bind to lipid were investigated, respectively. The results showed that the �� helical contents of the monomeric wild type apoA-��, apoA-��(S52C), apoA-��(N74C), apoA-��(L107C), apoA-��(K129C), and apoA-��(L195C)were 54��4%,49��4%,50��2%,51��6%,56��4%,52��3%,and 54��1%, respectively. There were no statistical significances between them (P>0.05). The free energy of denaturation (��G 0_D) of wild type apoA-�� was 10.5 kJ/mol. ��G 0_D of apoA-��(S52C)and apoA-��_ Milano decreased by 2.1 kJ/mol and ��G 0_D of apoA-��(K129C)increased by 1.6 kJ/mol, when compared with wild type apoA-��.Binding capacity of apoA-��(K129C)and apoA-��(L195C)to lipid exhibited significantly lower affinity lipid than that of wild type apoA-�� (P<0.05), whereas there was no significant difference between the other cysteine mutants(including apoA-��_ Milano ) and the wild type (P>0.05) has been observed. These results indicate that the cysteine mutations at the different sites have not significant effect on the �� helical content of apoA-��, but have different influence on its secondary structural stability and its ability to bind to lipids.
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Received 2004-11-24;
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ףѧ��.����֬����A-����װ���ͻ����Ķ����ṹ��֬�ʽ�������ıȽ� [J]  �й����ﻯѧ���������ѧ��, 2005,V21(05 ): 603-603
. [J]  Chinese Journal of Biochemistry and Molecular Biol, 2005,V21(05 ): 603-603
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http://cjbmb.bjmu.edu.cn/CN/     ��     http://cjbmb.bjmu.edu.cn/CN/Y2005/V21/I05 /603