Purification and Characterization of a Deoxyriboendonuclease from Mycobacterium smegmatis

• Published in: BMB reports Vol. 39; no. 2; pp. 140 - 144
• Main Authors: Mandal, Prajna (Bose Institute, Acaharya J. C. Bose Birth centenary Building, Calcutta, India), Chakraborty, Phulghuri (Bose Institute, Acaharya J. C. Bose Birth centenary Building, Calcutta, India), Sau, Subrata (Bose Institute, Acaharya J. C. Bose Birth centenary Building, Calcutta, India), Mandal, Nitai Chandra (Bose Institute, Acaharya J. C. Bose Birth centenary Building, Calcutta, India), E-mail: mandalnc2003@yahoo.com
• Format: Journal Article
• Language: English
• Published: Korea (South) 31.03.2006
• Subjects: BACTERIA; Deoxyriboendonuclease; Deoxyribonucleases - chemistry; Deoxyribonucleases - isolation & purification; DNA - chemistry; Enzyme Activation - physiology; Escherichia coli - enzymology; M. smegmatis; Molecular Weight; Mycobacteria; Mycobacterium smegmatis - enzymology; Oligonucleotides - chemistry
• ISSN: 1225-8687; 1976-6696; 0219-1024
• DOI: 10.5483/bmbrep.2006.39.2.140

A deoxyriboendonuclease has been purified to near homogeneity from a fast growing mycobacterium species, M. smegmatis and characterized to some extent. The size of enzyme is about 43 kDa as determined by a denaturing gel analysis. It shows optimum activity at 32℃ in Tris-HCl buffer (pH 7.2) containing 2.5 mM of MgCl₂. Both EDTA and K+ but not Na+ inhibit its activity. Evidences show that the enzyme is not a restriction endonuclease but catalyzes the endonucleolytic cleavage of both the double- as well as the single-strand DNA non-specifically.