EGTA公司
腺苷酸激酶
环化酶
化学
生物物理学
钙
生物化学
生物
酶
有机化学
作者
Julie A. Smith,Martin Griffin,Stewart E. Mireylees,Richard Long
出处
期刊:FEBS Letters
[Wiley]
日期:1993-07-26
卷期号:327 (2): 137-140
被引量:6
标识
DOI:10.1016/0014-5793(93)80157-p
摘要
This study demonstrates that the inhibition of adenylate cyclase activity by Ca2+ is enhanced in the presence of increasing [EGTA] (0, 0.3, 1, 2.5 mM) by 2 orders of magnitude. It has been established that this effect is not because of poor Ca2+ buffering by low [EGTA] or high Ca2+ binding by the membrane preparation. It is present irrespective of stimulus. We suggest the enhanced sensitivity of adenylate cyclase to Ca2+ induced by EGTA is caused by the Ca-EGTA complex being a more inhibitory species than Ca2+. Thus consideration of the effects of the Ca-EGTA complex should be made when interpreting the results from experiments involving Ca2+ and EGTA.
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