By Gebhard Koch
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Extra info for Biosynthesis, Modification, and Processing of Cellular and Viral Polyproteins
Sequential immunoprecipitation the cell-free synthesized 21 studies suggested that K product is the common precursor to Np II and vasopressin. The specificity of the immunoprecipitation was demonstrated by competition with excess amounts of unlabeled neurophysin II or vasopressin using the appropriate antiserum; no competition was observed with unlabeled neurophysin I, oxytocin or luteinizing hormone release hormone (LHRH). Experiments with membrane fractions strongly suggest that the 21 K polypeptide is the prepro-form of the Np II/AVP-precursor.
3, immunoprecipitation of cell-free synthesized proteins from wheat germ translations has yielded two major proteins specifically recognized by antibodies, a 2325,000 dalton species by anti-neurophysin II and a 17-18,000 dalton species by anti-neurophysin I. More recently, we have found that these same proteins are obtained in rabbit reticulocyte lysate translations. Discrimination of each of these proteins by a particular anti-neurophysin suggests that each contains a unique neurophysin type (either I or II).
The above mapping data, combined with those obtained for protein immunoprecipitated by anti-neurophysin I, serve to establish firmly that the 17-18,000 and 23-25,000 dalton translation products contain the sequences of neurophysins I and II, respectively. > 1971; Livett, 1978) that the hypothalamus is a site of biosynthesis of neurophysins and that these proteins are made as parts of precursors. Given these assertions, our finding of two unique proteins coded by total bovine hypothalamic mRNA provides compelling proof that neurophysins I and II are biosynthesized in the bovine species via initial translation products, definable as pre-pro-neurophysins, of 17-18,000 and 23-25,000 daltons, respectively.
Biosynthesis, Modification, and Processing of Cellular and Viral Polyproteins by Gebhard Koch