Malacinski G M, Konetzka W A
J Bacteriol. 1967 Jun;93(6):1906-10. doi: 10.1128/jb.93.6.1906-1910.1967.
Information was obtained on the general properties and specificity of orthophosphite-nicotinamide adenine dinucleotide oxidoreductase. The enzyme was extracted from Pseudomonas fluorescens 195 grown in medium containing orthophosphite as the sole source of phosphorus. An enzyme preparation suitable for characterization was obtained from crude extracts by use of high-speed centrifugation, protamine sulfate precipitation, ammonium sulfate fractionation, and Sephadex gel filtration. The enzyme exhibited maximal activity at pH 7.0, and was inactivated within 6 min at 37 C. Arsenite, hypophosphite, nitrite, selenite, and tellurite were not oxidized by the enzyme. Sulfite inhibited the enzymatic oxidation of orthophosphite in an apparent competitive manner.
获取了有关亚磷酸 - 烟酰胺腺嘌呤二核苷酸氧化还原酶的一般性质和特异性的信息。该酶是从在以亚磷酸作为唯一磷源的培养基中生长的荧光假单胞菌195中提取的。通过高速离心、硫酸鱼精蛋白沉淀、硫酸铵分级分离和葡聚糖凝胶过滤，从粗提物中获得了适合进行表征的酶制剂。该酶在pH 7.0时表现出最大活性，并在37℃下6分钟内失活。亚砷酸盐、次亚磷酸盐、亚硝酸盐、亚硒酸盐和亚碲酸盐不能被该酶氧化。亚硫酸盐以明显的竞争性方式抑制亚磷酸的酶促氧化。
