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Chemical Modification of Aeromonas hydrophila Extracellular Protease
CHU Wei hua,LU Cheng ping (Key Laboratory of Animal Disease Diagnostic and Immunology of Ministry of Agriculture, Nanjing Agricultural University,Nanjing\ 210095,China)
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ժҪ ����ø����ˮ���� (Aeromonashydrophila)����Ҫ�²����� .Ϊ�о���ṹ�빦��֮��Ĺ�ϵ ,��DEPC��EDC��PMSF��N AI�� 9�ֻ�ѧ���μ�������ˮ����J 1����⵰��øECPase54,Ȼ�������ø���� ,�����о�ø�����а��������������ø�������ĵĹ�ϵ .������ ,�Ȼ�˿���ᡢ�� �����һ�Ȳл���ø������ ;���װ���л���ø����Ҳ��ֱ�ӹ�ϵ ;��ɫ���ᡢ�鰱�ᡢ�Ұ���л�����Լ������Ļ�ѧ��������ø���ԵĴ��ȵ��½� ,˵��ɫ���ᡢ�鰱�ᡢ�Ұ���л��Լ��������ø���������Ļ���
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Abstract ��
Extracellular protease was one of the important pathogenic factors of Aeromonas hydrophila. In order to investigate the relationship of the structure and function of extracellular protease,the effects of protein modification reagents on the Aeromonas hydrophila extracellular protease ECPase54 activity have been studied.The protease was not affected by EDC,PMSF,2,3\|diacetyl and acetic anhydride modification,indicating that carboxyl groups,serine residues,guanidine groups and �� amino groups were non\|essential to the enzyme activity.The enzyme activity was significantly decreased after DEPC,NBS,N\|AI,2\|ME modification,and was slightly decreased after PCMB modification.These results indicated that the histidine residues,tryptophane residues,tyrosine residues and disulfides groups seemed to be essential to catalytic activity or located at the active site of ECPase54.
Keywords ��
Aeromonas hydrophila
extracellular protease
chemical modification
enzyme activity
Received 2000-09-11;
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