Creatine phosphate inhibition of adenylate deaminase is mainly due to pyrophosphate.
Creatine phosphate inhibition of adenylate deaminase is mainly due to pyrophosphate.
复制标题
磷酸肌酸对腺苷酸脱氨酶的抑制作用主要是由于焦磷酸盐。
DOI:
10.1016/s0021-9258(17)37794-3
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发表时间:
1979
期刊:
影响因子:
--
通讯作者:
J. Lowenstein
中科院分区:
文献类型:
--
作者:
T. J. Wheeler;J. Lowenstein
Inhibition of rat skeletal muscle adenylate deaminase by creatine phosphate reported previously is due to inorganic pyrophosphate present as a contaminant in commercial preparations of creatine phosphate. This conclusion is based on the following evidence: a compound that inhibits adenylate deaminase can be separated from commercially prepared creatine phosphate by ion exchange chromatography; the inhibition by “creatine phosphate” and by the separated inhibitory compound is relieved by treatment with inorganic pyrophosphatase; inhibition by inorganic pyrophosphate is similar to that produced by unpurified creatine phosphate; and pyrophosphate is present in commercially available creatine phosphate in amounts sufficient to account for the inhibition. Some commercial preparations of creatine phosphate contain much less pyrophosphate than others; these preparations are only weakly inhibitory. Inorganic triphosphate is a more powerful inhibitor of the enzyme than pyrophosphate; it may also be present as a contaminant in creatine phosphate.