Abstract
A ribosomal-pH 5 enzyme system prepared from bovine anterior pituitary glands was found to be active in the incorporation of isotopic amino acids into growth hormone and mixed proteins. A small scale modification of an existing procedure was employed for isolation of the labeled hormone, following incubation of the cell-free biosynthetic system in the presence of required cofaetors. The radioactive product was indistinguishable from authentic growth hormone standards by three physical criteria: Sephadex gel filtration, polyacrylamide disc gel electrophoresis, and sucrose density gradient centrifugation. In addition, it displayed immunological activity by binding specific antibody.
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