| Title | Partial characterization of proteases from culture filtrate of mycobacterium tuberculosis |
|---|---|
| Author | Na, Byoung Kuk¹ · Song, Chul Yong¹ * · Park, Young Kil² · Bai, Gill Han² · Ki, Sang Jae² |
| Address | ¹Department if Biology, Facult of Natural Science, Shung-Ang University; ²Korean Institute of Tuberculosis |
| Bibliography | Journal of Microbiology, 34(2),198-205, 1996, |
| DOI | |
| Key Words | Mycobacterium tuberculosis, characterization, proteases |
| Abstract | Two proteases were partially characterized from culture filtrate of Mycobacterium, tuberculosis KIT110. Their molecular weights were approximately 200 and 180 kDa, respectively and they exhibited similar enzymatic characteristics. These enzymes were inhibited significantly by EDTA and to some extent by EGTA. Their activity was enhanced by Ca^2+ and Mg^2+ to some degree. However, Cu^2+ and Ag^2+ completely inhibited the enzyme activity at the concentration of 2.5 and 5 mM, respectively. The optimal pH was 7.0 and optimal temperature was around 40℃. These enzymes were rapidly inactivated at 80℃. Therefore, they were heat-labile, neutral metalloproteases. These enzymes exhibited antigenicity shown by their reacting with sera from the partients with pulmonary tuberculosis. These enzymes were able to degrade serum proteins including hemoglobin, bovine serum albumin, lysozyme and immunoglobulin G and structural matrix protein such as type I collagen. Therefore, these enzymes may be thought to contribute to tissue necrosis and pathogenesis during infection. |
| Download PDF | Eng_340214_198-205p.pdf |