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[来自大鼠肝细胞核的组蛋白特异性乙酰转移酶]

[Histone-specific acetyltransferase from the rat liver nuclei].

作者信息

Tsudezevich B A, Roginets N B, Blium Ia B, Kucherenko N E

出版信息

Ukr Biokhim Zh (1978). 1985 Mar-Apr;57(2):67-9.

PMID:4002369
Abstract

Certain properties of histone-specific acetyltransferases A, B and C, obtained from the rat liver are determined. pH optimum for enzyme A is within the range of 7.5-8.5, for B--7.8 and for C--7.5. The maximal activity for enzymes A, B and C is observed with the 60 micrograms/ml concentration of the substrate. The activity is inhibited by N-maleimide, iodacetamide and chloromercuribenzoate. The results obtained show that a number of similar properties are typical of the above enzymes.

摘要

测定了从大鼠肝脏中获得的组蛋白特异性乙酰转移酶A、B和C的某些特性。酶A的最适pH在7.5 - 8.5范围内,酶B为7.8,酶C为7.5。当底物浓度为60微克/毫升时,观察到酶A、B和C的最大活性。该活性受到N - 马来酰亚胺、碘乙酰胺和对氯汞苯甲酸的抑制。所得结果表明,上述酶具有许多相似的特性。

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