Purification and some properties of carbonic anhydrase from bovine skeletal muscle |
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| Authors: | P Engberg E Millqvist G Pohl S Lindskog |
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| Affiliation: | 1. Department of Biochemistry University of Umeå, S-901 87 Umeå, Sweden;1. Department of Medical and Physiological Chemistry, University of Umeå, S-901 87 Umeå, Sweden;1. Laboratory of Biochemistry and Neuroscience, Team of Applied Biochemistry and Toxicology, Faculty of Science and Technology, University Hassan First, 577 Settat, Morocco;2. College of Education, Bayburt University, 69000 Bayburt, Turkey;3. Chemistry Education, Kazim Karabekir Education Faculty, Atatürk University, 25240 Erzurum, Turkey;1. Laboratory of Biochemistry and Neuroscience, Team of Applied Biochemistry and Toxicology, Faculty of Science and Technology, University Hassan First, 577, Settat, Morocco;2. College of Education, Bayburt University, 69000, Bayburt, Turkey;3. Department of Nanoscience and Nanoengineering, Institute of Science, Atatürk University, 25240, Erzurum, Turkey;4. Chemistry Education, Kazim Karabekir Education Faculty, Atatürk University, 25240, Erzurum, Turkey;1. Department of Chemistry, Louisiana State University, Baton Rouge, LA, 70803, USA;2. Department of Chemistry and Biochemistry, Baylor University, Waco, TX, 76706, USA;1. Signalisation et Transports Ioniques Membranaires, Université de Poitiers, CNRS ERL 7368; 1 rue Georges Bonnet F-86073 Poitiers Cedex 09, France;2. Laboratoire de Physiologie Animale, Université de Ouagadougou, 03 BP 7021, Ouagadougou 01, Burkina Faso;3. Superacid group in “Organic Synthesis” team, Université de Poitiers, CNRS UMR 7285 IC2MP, 4 avenue Michel Brunet, Poitiers 86022 Cedex, France;4. Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino (Firenze), Italy |
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| Abstract: | Procedures for the purification of bovine muscle carbonic anhydrase (isoenzyme III) are described. The purified enzyme has a molecular weight near 29,000 and contains one Zn2+ ion per molecule. The sedimentation coefficient, s(0)20,w, is 2.8 X 10(-13) s, the isoelectric pH is 8.5, and A280(0.1%) = 2.07 cm-1. The CO2 hydration activity, expressed as kcat/Km, is about 1.5% of that of human isoenzyme I (or B) and about 0.3% of that of human isoenzyme II (or C) at pH 8 and 25 degrees C. The activity is nearly independent of pH between pH 6.0 and 8.6. The muscle enzyme is weakly inhibited by the sulfonamide inhibitor, acetazolamide, whereas some anions, particularly sulfide and cyanate, are efficient inhibitors. Bovine carbonic anhydrase III contains five thiol groups, two of which react readily with Ellman's reagent without effect on the catalytic activity. A reinvestigation of the amino acid sequences of cysteine-containing tryptic peptides has shown that cysteine residues occur at sequence positions 66, 183, 188, 203, and 206. |
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