<1> AN PREV199800046414 AU Bagchi Divya. Verma Deepti. "IN Dep. Biol. Sci., R.D. Univ., Jabalpur 482001, India." TI Partial purification and regulation of sulfur metabolizing enzymes in a cyanobacterium Phormidium uncinatum. "SO Indian Journal of Experimental Biology. 35(8). Aug., 1997. 876-880. " "AB Phormidium uncinatum CU 1462/7 was able to grow with several sulfur compounds. The sulfur metabolizing enzymes, viz. ATP sulfurylase, cysteine synthase. L- and D- cysteine desulfydrases and thiosulfate reductase were regulated by sulfur sources, particularly by sulfur amino acids and thiol containing compounds. Sulfur starvation caused reduction in ATP sulfurylase activity, while the levels of other enzymes activities were appreciated. These enzymes were purified by conventional techniques using DEAE Cellulose and Blue Sepharose columns. The specific activities increased in the range of 100-150-folds. With partially purified enzymes, apparent Km values for sulfate, ATP, D and L-cysteines, thiosulfate, sulfide and acetyl serine were 10, 25, 30, 80, 100, 5 and 25 muM respectively." <2> AN PREV199799697168 AU Bagchi Divya. Verma Deepti. "IN Dep. Biol. Sci., R.D. Univ., Jabalpur 482 091, India." "TI Selenate-regulation of sulfur metabolism in a cyanobacterium, Phormidium uncinatum." SO Journal of Plant Physiology. 150(6). 1997. 762-764. "AB Selenate-mediated regulation of sulfate assimilation was studied in Phormidium uncinatum and its selenate resistant mutant. Selenate-caused suppression of sulfate-supported wild type growth was due to inactivation of ATP-sulfurylase activity. Mutation led to loss of this enzyme and growth with sulfate; therefore, thiosulfate served as sulfur source. Both strains grew with several alternate sulfur sources, cysteine and methionine included. L-cysteine repressed sulfurylase and cysteine synthase but activated its desulfhydrase and thiosulfate reductase activities. Mutant enzymes were deregulated for activation."