Purification and characterization of carbonic anhydrase from the saliva of the rat.
作者： J B Feldstein , D N Silverman
DOI: 10.1016/S0021-9258(18)91031-8
关键词: Isozyme 、 Isoelectric point 、 Turnover number 、 Saliva 、 Carbonic anhydrase 、 Molecular biology 、 Steady state (chemistry) 、 Carbonic anhydrase II 、 Concanavalin A 、 Biochemistry 、 Chemistry
摘要: Carbonic anhydrase purified from the saliva of rat had kinetic properties identical with those carbonic II red cells, but its molecular were distinctly different type isozyme. Kinetic parameters measured under steady state conditions by stopped-flow spectrophotometry and equilibrium an 18O exchange method. The turnover number kcat for hydration CO2 was 6.5 X 10(4) s-1 Michaelis constant 4.2 mM at pH 7.5 25 degrees C, values which are equal to constants cell rat. Inhibition salivary isozyme sulfanilamide (Ki = 3.7 microM) nearly as efficient inhibition erythrocyte 1.1 microM). weight 46,000 isoelectric point 5.5. Salivary high mannose oligosaccharide components concanavalin A binding. amino acid composition not similar II, it that reported membrane-bound bovine lung (Whitney, P.L., Briggle, T.V. (1982) J. Biol. Chem. 257, 12056-12059). These observations suggest us is a secretory product.
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