Isolation and partial characterization of two alkaline proteases of the greater wax moth Galleria mellonella (L.) |
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| Institution: | 1. Institute of Pharmacy and Molecular Biotechnology, Heidelberg University, INF 364 Heidelberg, Germany;2. Department of Medical Laboratory Technology, Faculty of Medical Technology, Baghdad, Iraq;3. Department of Infectious Diseases, Medical Microbiology and Hygiene, Heidelberg University, INF 324 Heidelberg, Germany;1. Department of Otolaryngology, Meir Hospital, Kfar Saba, Israel;2. Department of Biomedical Engineering, Virginia Commonwealth University, Richmond, VA, United States;3. School of Art, Virginia Commonwealth University, Richmond, VA, United States;4. University of Texas Health Science Center at San Antonio, San Antonio, TX, United States;5. Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA, United States |
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| Abstract: | Two alkaline proteases were isolated from whole-body extracts of Galleria mellonella larvae. The two proteases were separated by cation-exchange chromatography on CM-Sepharose CL6B and further purified by gel filtration on Ultrogel ACA 54. The optimal pH of activity using Azocoll as substrate was 10.5 for protease P-1 and 11.2 for protease P-2. The molecular weights of the two enzymes determined by gel filtration were respectively 12,500 and 10,500. Protease P-1 was inhibited by soybean trypsin inhibitor, TPCK, TLCK and activated by non-ionic detergents. Protease P-2 was inhibited by soybean trypsin inhibitor, 4-aminobenzamidine, ovomucoid and activated by dithiothreitol. Both enzymes were partially inhibited by PMSF.Distribution studies suggested that the two proteases were digestive enzymes. |
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