A cysteine desulfhydrase was purified 110-fold from the green alga Chlorella using conventional techniques. The isolated cysteine desulfhydrase was specific for ᴅ-cysteine having no activity towards ʟ-cysteine. ᴅ- and ʟ-cysteine desulfhydrase activities can be separated using DEAE-cellulose chromatography techniques. The isoelectric point of this enzyme was determined to be around a pH of 4.5 using a chromatofocussing column. The pH-optimum for the ᴅ-cysteine desulfhydrase was found to be in the range of 8.5 to 9 and the apparent Kᴍ for ᴅ-cysteine was determined to 0.16 mᴍ. The enzyme was active without addition of metal ions and EDTA or citric acid did not inhibit this activity.
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