Shirazi S P, Beechey R B, Butterworth P J
Biochem J. 1981 Mar 15;194(3):797-802. doi: 10.1042/bj1940797.
The inhibition by phosphonates and phosphate analogues of the alkaline phosphatase activity of rat intestinal brush-border membrane vesicles was studied at pH 7.5 and 30 degrees C. Phenylene-1,3-diphosphonate, 2,6-dinitrophenylphosphonate and phosphonoacetaldehyde were found to be competitive inhibitors, with Ki values in the range 16-80 microM. Adenosine 5'-[beta-thio]diphosphate and adenosine 5'[gamma-thio]triphosphate are also very potent inhibitors, with Ki values of approx. 10 microM. The inhibition produced by these thiophosphates was mainly competitive but with a slight non-competitive element. Adenosine 5'-[beta gamma-imido]triphosphate is also a competitive inhibitor of the alkaline phosphatase, but oxidation of the ribose moiety of this compound with NaIO4 results in an active-site-directed irreversible inhibitor that could be of general use in studies of the mechanism of action of this enzyme.
在pH 7.5和30℃条件下，研究了膦酸盐和磷酸类似物对大鼠肠刷状缘膜囊泡碱性磷酸酶活性的抑制作用。发现亚苯基-1,3-二膦酸盐、2,6-二硝基苯基膦酸盐和膦酰乙醛是竞争性抑制剂，其Ki值在16 - 80 microM范围内。腺苷5'-[β-硫代]二磷酸和腺苷5'-[γ-硫代]三磷酸也是非常有效的抑制剂，Ki值约为10 microM。这些硫代磷酸盐产生的抑制作用主要是竞争性的，但有轻微的非竞争性成分。腺苷5'-[βγ-亚氨基]三磷酸也是碱性磷酸酶的竞争性抑制剂，但是用NaIO4氧化该化合物的核糖部分会产生一种活性位点导向的不可逆抑制剂，这种抑制剂可能普遍用于该酶作用机制的研究。
