Komarova Iu M, Terekhova I V, Doman N G, Al'bitskaia O N
Biokhimiia. 1976 Jan;41(1):183-7.
Carboanhydrase (carbonate-hydroliase EC 4.2.1.1.) is found in the extract of Spirulina platensis cells. A linear dependency of the enzyme activity on the protein concentration; pH optimum is found to be 8.0. Specific activity of carboanhydrase is 3 muM/min-mg of protein under the concentration of CO2 of 4-10(-3) M, appearing Michelis constant being 4.9-10(-3) M. The enzyme was stabilized with 10 mM of cisteine, its activity was inhibited by 50% with sulphanylamide (1-10(-5) M), acetazolamide (8--10(-7) M) and Cl- ions (5-10(-2) M). The activity of carboanhydrase, as well as the rate of NaH14CO3 fixation, depended on the pH value of cultural medium.
碳酸酐酶(碳酸水解酶,EC 4.2.1.1.)存在于钝顶螺旋藻细胞提取物中。酶活性与蛋白质浓度呈线性相关;最适pH值为8.0。在二氧化碳浓度为4×10⁻³ M时,碳酸酐酶的比活性为3 μM/(min·mg蛋白质),米氏常数为4.9×10⁻³ M。该酶用10 mM半胱氨酸稳定,其活性被磺胺(1×10⁻⁵ M)、乙酰唑胺(8×10⁻⁷ M)和Cl⁻离子(5×10⁻² M)抑制50%。碳酸酐酶的活性以及NaH¹⁴CO₃固定速率取决于培养基的pH值。