The purification and subunit structure of cysteine desulfhydrase from Salmonella typhimurium.
نویسندگان
چکیده
The inducible enzyme, cysteine desulfhydrase, was purified from Salmonella fyphimurium to a state of near homogeneity. This enzyme has a very low tryptophanase activity, lacks cystathionase and tryptophan synthetase activities, and appears to be a specific cysteine desulfhydrase. The purified native enzyme has an s20,W of 10.4 and a molecular weight of 229,000 as determined by equilibrium sedimentation. Polyacrylamide electrophoresis in sodium dodecyl sulfate showed a single species of polypeptide chain with a molecular weight of 37,000 while the pyridoxal phosphate content was found to be 1 mole per 37,700 g of protein. These data, together with the results of amino acid analyses, tryptic peptide maps, and an NH2-terminal amino acid analysis, indicate that the native enzyme is a hexamer, containing 6 moles of pyridoxal phosphate, and composed of six identical polypeptide chains with NH2-terminal serines.
منابع مشابه
Cysteine catabolism and cysteine desulfhydrase (CdsH/STM0458) in Salmonella enterica serovar typhimurium.
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#To whom correspondence should be addressed: Larry Reitzer, Department of Molecular and 10 Cellular Biology, University of Texas at Dallas, RL11, 800 West Campbell Rd, Richardson, TX 11 75080 Phone: (972) 883-2502, Fax: (972) 8832409, Email: [email protected] 12 13 Cysteine is potentially toxic and can affect diverse functions such as oxidative stress, 14 antibiotic resistance, and swarming ...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 247 22 شماره
صفحات -
تاریخ انتشار 1972