Purification and properties of the carbonic anhydrase of Rhodospirillum rubrum |
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| Authors: | Steven R. Gill Paula J. Fedorka-Cray Rodney K. Tweten Bayard P. Sleeper |
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| Affiliation: | (1) Department of Bacteriology, North Dakota State University, 58105 Fargo, ND, USA;(2) Present address: Division of Biology, Kansas State University, 66506 Manhattan, KS, USA;(3) Present address: Department of Geographic Medicine, Baltimore City Hospital, Johns Hopkins University, 21224 Baltimore, MD, USA;(4) Present address: Department of Microbiology, University of California at Los Angeles, 90024 Los Angeles, CA, USA |
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| Abstract: | The carbonic anhydrase (EC 4.2.1.1) of Rhodospirillum rubrum has been purified to apparent homogeneity and some of its properties have been determined. The enzyme was cytoplasmic and was found only in photosynthetically grown cells. It had a molecular weight of about 28,000, and was apparently composed of two equal subunits. The amino acid composition was similar to that of other reported carbonic anhydrases except that the R. rubrum enzyme contained no arginine. The isoelectric point of the enzyme was 6.2 and the pH optimum was 7.5. It required Zn(II) for stability and enzymatic activity. The Km(CO2) was 80 mM. Typical carbonic anhydrase inhibition patterns were found with the R. rubrum enzyme. Strong acetazolamide and sulfanilamide inhibition confirmed the importance of Zn(II) for enzymatic activity as did the anionic inhibitors iodide, and azide. Other inhibitors indicated that histidine, sulfhydryl, lysine and serine residues were important for enzymatic activity.Abbreviation CA carbonic anhydraseIn memory of R. Y. Stanier |
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| Keywords: | Carbonic anhydrase Rhodospirillum rubrum Carbonic anhydrase purification Carbonic anhydrase properties |
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