Salt inhibition of nuclear histone acetyltransferase from calf thymus.

L J Wong, W F Patton
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Abstract

Nuclear histone acetyltransferase isolated from calf thymus was found to be inhibited by numerous salts at millimolar concentrations. Salts made up of monovalent ions caused 50% decrease in enzymatic activity at an average concentration of 51 +/- 14 mM while the same degree of inhibition was achieved by divalent salts at 15 +/- 5 mM. At the same ionic strength in the range from 5 to 70 mM, the divalent salts were 14-31% more inhibitory than the salts of monovalent ions. Kinetic analysis showed that NaCl and (NH4)2SO4 inhibited the enzyme competitively against both acetyl-CoA and histones. The inhibition constants for NaCl against acetyl-CoA and histones are respectively 30 and 34 mM. That for (NH4)2SO4 are 8 and 12 mM respectively.

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盐对小牛胸腺核组蛋白乙酰转移酶的抑制作用。
从小牛胸腺分离的核组蛋白乙酰转移酶被许多毫摩尔浓度的盐所抑制。在平均浓度为51 +/- 14 mM时,一价盐的酶活性降低50%,而在平均浓度为15 +/- 5 mM时,二价盐的抑制程度相同。在5 ~ 70 mM的相同离子强度范围内,二价盐比一价盐的抑制程度高14-31%。动力学分析表明,NaCl和(NH4)2SO4对乙酰辅酶a和组蛋白均有竞争性抑制作用。NaCl对乙酰辅酶a和组蛋白的抑制常数分别为30和34 mM,对(NH4)2SO4的抑制常数分别为8和12 mM。
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