Biosynthesis, Modification, and Processing of Cellular and by Gebhard Koch

By Gebhard Koch

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Acad. Sei. USA 77, n°5. , and Herbert, E. (1977). PWC. Hatl. Acad. Scl. USA 74, 5300. , and Gainer, H. (1979). PKOC. hlatl. Acad. Sei. USA 76, 6086. , and Takabatake, Y. (1964). EndocAlnology 75, 943. , and Richter, D. (1979). Fed. Eu&. Blochom. Soc. Lett. /OS, 311. , and Sachs, H. (1964). EndocAlnology 75, 934. Biosynthesis, Modification, and Processing of Cellular and Viral Polyproteins ON THE BIOSYNTHETIC ORIGIN OF NEUROPHYSIN-NEUROHYPOPHYSEAL PEPTIDE HORMONE COMPLEXES Christopher J. Hough Paul A.

Less efficient in translating hypothalamic mRNA than the reticulocyte lysate system. Analysis of the translation products by SDS gel electrophoresis revealed that in the wheat germ system particularly the high molecular weight proteins were missing (Fig. 2 ) . Comparison of reticulocyte lysate systems from New England Nuclear, Boston and Amersham, Braunschweig, indicated no differences in the efficiency of translating hypothalamic mRNA. However, in the lysate system from New England Nuclear but not in that from Amersham an unspecific polypeptide was synthesized that co-precipitated with anti Np I or anti OT and migrated close to the position of the OT-Np I precursor.

6 shows that, aside from the early radio-labeled peak derived from a combination of S-cysteic acid and as yet uncharacterized but largely non-specific small peptides, the most outstanding labelled peaks migrate identically with neurophysin peptides. Furthermore, the amount of radioactivity in each major neurophysin-related peak is as expected based on the content of cysteine in authentic fragments; thus, co-migration of hormone-related peptides within neurophysin peaks is unlikely. 5 minutes, are not neurophysinrelated.

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