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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Reddy A V, DeLange R J

Int J Biochem. 1982;14(6):477-82. doi: 10.1016/0020-711x(82)90115-x.

Protamines were preferentially phosphorylated by the six protein kinase fractions isolated from calf thymus nuclear sap, but histones with the exception of H4 also proved to be acceptable substrates. 2. BSA was not a substrate for the first five kinase fractions, but was the best substrate for the seventh fraction, which also exhibited considerable activity with H4 as substrate. 3. An analysis of in vitro phosphorylation experiments with nuclear sap protein kinases reveals a decreased H2b phosphorylation in H1-depleted chromatin relative to "native" chromatin. 4. With fraction V the initial velocity patterns at fixed ATP levels and varying concentrations of histones exhibit cooperativity at lower concentrations and inhibition at higher concentrations, indicating that nuclear sap kinases might play important roles in sensitive regulatory mechanisms of histone phosphorylation in vivo.

从小牛胸腺核液中分离出的六种蛋白激酶组分可优先使鱼精蛋白磷酸化，但除H4外的组蛋白也被证明是合适的底物。2. 牛血清白蛋白（BSA）不是前五个激酶组分的底物，但却是第七个组分的最佳底物，该组分以H4为底物时也表现出相当的活性。3. 对核液蛋白激酶的体外磷酸化实验分析表明，相对于“天然”染色质，H1缺失的染色质中H2b磷酸化减少。4. 对于组分V，在固定ATP水平和不同组蛋白浓度下的初始速度模式在较低浓度下表现出协同性，在较高浓度下表现出抑制作用，这表明核液激酶可能在体内组蛋白磷酸化的敏感调节机制中发挥重要作用。

Reddy A V, DeLange R J

Int J Biochem. 1982;14(6):477-82. doi: 10.1016/0020-711x(82)90115-x.

Protamines were preferentially phosphorylated by the six protein kinase fractions isolated from calf thymus nuclear sap, but histones with the exception of H4 also proved to be acceptable substrates. 2. BSA was not a substrate for the first five kinase fractions, but was the best substrate for the seventh fraction, which also exhibited considerable activity with H4 as substrate. 3. An analysis of in vitro phosphorylation experiments with nuclear sap protein kinases reveals a decreased H2b phosphorylation in H1-depleted chromatin relative to "native" chromatin. 4. With fraction V the initial velocity patterns at fixed ATP levels and varying concentrations of histones exhibit cooperativity at lower concentrations and inhibition at higher concentrations, indicating that nuclear sap kinases might play important roles in sensitive regulatory mechanisms of histone phosphorylation in vivo.

从小牛胸腺核液中分离出的六种蛋白激酶组分可优先使鱼精蛋白磷酸化，但除H4外的组蛋白也被证明是合适的底物。2. 牛血清白蛋白（BSA）不是前五个激酶组分的底物，但却是第七个组分的最佳底物，该组分以H4为底物时也表现出相当的活性。3. 对核液蛋白激酶的体外磷酸化实验分析表明，相对于“天然”染色质，H1缺失的染色质中H2b磷酸化减少。4. 对于组分V，在固定ATP水平和不同组蛋白浓度下的初始速度模式在较低浓度下表现出协同性，在较高浓度下表现出抑制作用，这表明核液激酶可能在体内组蛋白磷酸化的敏感调节机制中发挥重要作用。