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EuA. J. Blochom. 78, 337. , and Cohen, P. (1979). Fed. Eat. Blochom. Soc. LoXt. 108, 369. Camier, M. et al. (1980), ixi pKCpa&CUtion. , and Camier, M. (1979). In "Current Topics in Cellular Regulation11 15, 263. , and Chretien, M. (1978). VfiOC. UcuUL. Acad. Scl. USA 75, n°10, 4719. B. (1968). Blochom. 4106, 565. E. (1978). J. Blol. Chew. 151, 5732. , and Sachs, H. (1968). Endoc/Unology 83, 1299. Gainer, H. , and Same, Y. (1977a). In "Peptides in Neurobiology" (H. ), p. 183. Plenum, New York). Gainer, H.

CaLLbticubLon wa* done with ziabblt IgG 1150,000;a) 12S I-labeled ovalbumln [4S,000;b] HGH (22,000;c) and neu&ophyAln [10,000id). , 19S0, by peAmu&lon). as Mr 70,000 species (Fig. 3A). This transformation from apparent Mr 140,000 to 70,000 was both quantitative and reversible (Fig. 3B). The peculiar behaviour of this material is not yet clear : it might be related to the presence of carbohydrate BIOSYNTHETIC PRECURSORS OF NEUROHORMONES TG I 50 IgG SAB \ 21 Np I I 60 70 80 90 S W > 96 i6b i\b lift l4ö Uö IG T Fractions I Tterrtor Fractions FIGURE 3.

9 19681. 9 1971). , 19751 as a sort of "ribonuclease S of the pituitary,ff which derives from a covalent parent, containing one hormone and one neurophysin, by limited post-translational proteolysis. , 1975;ttenendez-Botetand Breslow, 1975) have added to the evidence that these proteins are indeed produced via biosynthetic precursors. 31 BIOSYNTHETIC ORIGIN However, while the above hypothesis about neurophysinpeptide biosynthesis has been stimulating to those of us interested in the biochemistry of these peptide-protein complexes, there has been a disquieting lack of rigorous chemical evidence to support it.

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