Studies on a membrane-bound and solubilized ribonucleotide reductase preparation from Escherichia coli TAU-.
Ribonucleotide reductase has been shown to be associated with the DNA-membrane complex in Escherichia coli TAU- cells. The membrane-bound enzyme has been released in a soluble form using a combined treatment of 1% sarcosyl (pH 8.0) and 1% sodium deoxycholate (pH 6.5). Allotropic differences in the modulatory effects of ATP, Mg2+, EDTA and dithiothreitol on the membrane-bound and solubilized enzyme activity are discussed.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology*; D003840:Deoxycholic Acid / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D007850:Lauric Acids / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D012264:Ribonucleotide Reductases / Q000378:metabolism*; D012521:Sarcosine / Q000031:analogs & derivatives / Q000494:pharmacology; D012995:Solubility
D003902:Detergents; D007850:Lauric Acids; D003840:Deoxycholic Acid; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D012264:Ribonucleotide Reductases; D008274:Magnesium; D004229:Dithiothreitol; D012521:Sarcosine