Partial purification and characterization of protein tyrosine kinases from normal tissues.

Partial purification and characterization of protein tyrosine kinases from normal tissues.
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正常组织中蛋白酪氨酸激酶的部分纯化和表征。

DOI:
10.1016/0003-9861(86)90602-8
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发表时间:
1986
影响因子:
3.9
通讯作者:
Racker,E
Racker,E
中科院分区:
生物学3区
文献类型:
--
作者:
Braun,S;AbdelGhany,M;Lettieri,JA;Racker,E

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相似文献

从人胎盘和猪脑中部分纯化了三种膜蛋白酪氨酸激酶(PTK)。两种胎盘酶(PTK-1和-2)在去污剂中的溶解度、分子量和酶性质方面不同。脑蛋白酪氨酸激酶在分子量和某些动力学性质方面类似于胎盘PTK-1。然而,Mn 2+对脑PTK的刺激大于Mg 2+,而Mg 2+对胎盘PTK-1的刺激率高于Mn 2+。0.1mNaCl对三种酶的抑制率均在50%左右。体外培养的抗脑酶的单克隆抗体抑制脑PTK和胎盘PTK-2,但对PTK-1或pp 60 src没有作用。因此,这三种酶似乎是动力学和免疫学上彼此不同的不同实体。用合成的酪氨酸-谷氨酸聚合物作为底物,可以在膜的粗提物中检测蛋白酪氨酸激酶活性。
Three membranous protein tyrosine kinases (PTKs) have been partially purified from human placenta and pig brain. The two placental enzymes (PTK-1 and -2) are distinct with respect to solubility in detergents, molecular weight, and enzymatic properties. The brain protein tyrosine kinase resembles placental PTK-1 with respect to molecular weight and some kinetic properties. However, stimulation of brain PTK is greater with Mn2+than with Mg2+whereas placental PTK-1 gives higher rates with Mg2+than with Mn2+. All three enzymes are inhibited about 50% by 0.1mNaCl. A monoclonal antibody raisedin vitroagainst the brain enzyme inhibits brain PTK as well as placental PTK-2, but has no effect against PTK-1 or pp60src. It thus appears that these three enzymes are distinct entities that differ from each other both kinetically and immunologically. With synthetic tyrosine-glutamic acid polymers as a substrate, protein tyrosine kinase activity can be detected in crude extracts of membranes.
从蛋白质样品中去除 Triton X-100 的简单程序。
DOI: --
发表时间: 1973
影响因子: 2.9
作者:
P. W. Holloway
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正常非增殖细胞中的高酪氨酸激酶活性
DOI: 10.1038/305435a0
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期刊: Nature
影响因子: 64.8
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DOI: --
发表时间: 1983
影响因子: 4.8
作者:
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DOI: --
发表时间: 1977
期刊: Biochemistry
影响因子: 2.9
作者:
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DOI: 10.1016/b978-0-12-442702-0.50023-6
发表时间: 1981
期刊: Acta Chemica Scandinavica
影响因子: --
作者:
G. Köhler
通讯作者: G. Köhler