A PLACENTAL POLYPEPTIDE ACTIVATOR OF A MEMBRANOUS PROTEIN-KINASE AND ITS RELATION TO HISTONE-1

被引：16

作者：

ABDELGHANY, M ^{[1
]}

RIEGLER, C ^{[1
]}

RACKER, E ^{[1
]}

机构：

[1] CORNELL UNIV, DIV BIOL SCI, BIOCHEM MOLEC & CELL BIOL SECT, ITHACA, NY 14853 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES | 1984年 / 81卷 / 23期

关键词：

D O I：

10.1073/pnas.81.23.7388

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Crude transforming growth factor preparations of human placenta contain a polypeptide that is required for the activity of a protein kinase purified from plasma membrane preparations of Ehrlich ascites tumor cells. The kinase activator was separated from transforming growth factor-.beta. by reversed-phase high-performance liquid chromatography and affinity chromatography. Like the transforming growth factor, it is heat stable and trypsin labile, but it is not inactivated by dithiothreitol. In sodium dodecyl sulfate/polyacrylamide gel electrophoresis the purified preparation shows a major double band at about 31,000 daltons. Comparisons of electrophoretic mobility, protein kinase stimulatory activity, and cross-reactivity with an antibody against histone 1 suggest that the placental activator is identical with histone 1.

引用

页码：7388 / 7391

页数：4

共 16 条

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