Acta Chimica Sinica ›› 2007, Vol. 65 ›› Issue (7): 651-654. Previous Articles    



黄小丽1, 汪开毓*,1, 苏秀梅1, 耿毅1, 邓永强2   

  1. (1四川农业大学动物科技学院鱼病研究中心 雅安 625014)
    (2四川省动物防疫监督总站 成都 610041)
  • 收稿日期:2006-07-28 修回日期:2006-11-27 出版日期:2007-04-14 发布日期:2007-04-14
  • 通讯作者: 汪开毓

Chemical Modification of Extracellular Protease of Stenotrophomonas maltophilia

HUANG Xiao-Li1; WANG Kai-Yu*,1; SU Xiu-Mei1; GENG Yi1; DENG Yong-Qiang2   

  1. (1 Fish Disease Research Center, College of Animal Science & Technology, Sichuan Agricultural University, Ya'an 625014)
    (2 Sichuan Provincial Office of Animal Disease Prevention and Control, Chengdu 610041)
  • Received:2006-07-28 Revised:2006-11-27 Online:2007-04-14 Published:2007-04-14
  • Contact: WANG Kai-Yu

Extracellular protease was one of the important pathogenic factors of Stenotrophomonas maltophilia. In order to investigate the relationship of structure and function of extracellular protease, the effects of protein modification reagents on the S. maltophilia extracellular protease activity have been studied. The chemical modification of extracellular protease of S. maltophilia was studied with phenylmethanesulfonyl fluoride (PMSF), p-chloromercuribenzoate (PCMB), N-acetylimidazole (N-AI), chloramine-T (Ch-T), N-bromosuccinimide (NBS), 2-mercaptoethanol (2-ME) as the modification reagents. The results indicated that the protease was not affected by N-AI, PMSF and PCMB, but Ch-T, NBS and 2-ME could reduce the activity significantly. It implied that Ser, Tyr and sulfhydryl residues were not activity dependent groups, while Met, Trp and disulfide linkage groups played an important role in the activity of extracellular protease. Meanwhile, EDTA, Mg2+, Ca2+, Hg2+ and Cu2+ could reduce the activity obviously, which showed that the enzyme was a metalloproteinase.

Key words: Stenotrophomonas maltophilia, extracellular protease, chemical modification