Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 0364819910290030167
Korean Journal of Microbiology
1991 Volume.29 No. 3 p.167 ~ p.171
Purification and Characterization of an Intracellular Protease from Pseudomonas carboxydohydrogena
Lee Hye-Soog

Kim Young-Min
Abstract
1
An intracellular protease from cells of Pseudomonas carboxydohydrogena grown on nutrient broth was purified to better than 95% homogeneity in five steps using azocaseine as a substrate. The molecular weight of the native enzyme was determined to be 125,000. Sodium dodecyl sulfate-gel electrophoresis revealed at least two non-identical subunits of molecular weight 70,000 and 56,000. The enzyme activity was completely inhibited by phenylmethylsulfonyl fluoride and diisopropyl fluorophosphate. The enzyme was also inhibited by Mgt+, Zn2+, Cd2+, Cue+, and Fee+, but was stimulated by iodoacetamide. Maximal reaction rate of the enzyme was observed at pH 8.0 and 30C. The isoelectric point of the enzyme was found to be 7.5. The enzyme was unable to hydrolyze carbon monoxide dehydrogenase.
KEYWORD
FullTexts / Linksout information
 
Listed journal information
ÇмúÁøÈïÀç´Ü(KCI)