Partial purification and characterization of protein tyrosine kinases from normal tissues.
Partial purification and characterization of protein tyrosine kinases from normal tissues.
复制标题
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
复制
发表时间:
1986
影响因子:
3.9
通讯作者:
Racker,E
中科院分区:
文献类型:
--
作者:
Braun,S;AbdelGhany,M;Lettieri,JA;Racker,E
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.
登录
查看更多内容
影响因子:
2.9
作者:
P. W. Holloway
通讯作者:
P. W. Holloway
影响因子:
64.8
作者:
F. Tuy;J. Henry;C. Rosenfeld;A. Kahn
通讯作者:
A. Kahn
影响因子:
4.8
作者:
G. Swarup;J. Dasgupta;D. Garbers
通讯作者:
D. Garbers
影响因子:
2.9
作者:
V. Yue;P. Schimmel
通讯作者:
P. Schimmel
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