Partial purification and biological activity of the product of chemically synthesized human growth hormone gene expression in Escherichia coli.

Abstract

The product of chemically synthesized human growth hormone gene expression in Escherichia coli was partially purified and proved to be identical with human growth hormone in size, in mobility on non-denaturing polyacrylamide gel electrophoresis, in behabior on HPLC, in immunological properties, and in biological activity in hypophysectomized rats.