DNA binding proteins of rat thigh muscle: Purification and characterization of an endonuclease

• Published in: Zeitschrift für Naturforschung C. A journal of biosciences Vol. 10; no. 1; pp. 85 - 94
• Main Authors: Augustine Rajakumar, AR, Shanmugam, G
• Format: Journal Article
• Language: English
• Published: 01-01-1986
• Subjects: DNA; endonuclease; muscles; proteins; rats
• ISSN: 0939-5075

Two major DNA binding proteins of molecular weights 34,000 and 38,000 have been identified in the 30,000 g supernatant (S-30) fraction of rat thigh muscle extracts. The 38 KD DNA binding protein differed from the 34 KD DNA binding protein also in its chromatographic behaviour. Prolonged incubation (30 days) of the 0 multiplied by 15 M NaCl eluates containing the two DNA binding proteins at 4 degree C led to the preferential degradation of the 34 KD DNA binding protein. Nitrocellulose filter binding assays indicated selective binding of purified 34 KD protein to ss DNA. Purified 34 KD DNA binding protein cleaved pBR 322 supercoiled DNA, and electrophoresis of the cleavage products in agarose gels revealed a major DNA band corresponding to the circular form of DNA.