Synthesis and partial maturation of the α‐ and γ‐subunits of the mouse submaxillary gland nerve growth factor in Xenopus laevis oocytes

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Abstract
Sera raised against the α-, β- and γ-subunits of the mouse 7 S NGF were used to characterize translation products coded by submaxillary gland mRNAs microinjected into Xenopus oocytes. Anti-βNGF sera did not cross-react with any material. In contrast, the precursors of the α- and γ-subunits, as well as that of renin were identified. Use of tunicamycin, and a comparison of the translation products obtained in oocytes or in the reticulocyte lysate indicated that oocytes achieved the cleavage of signal sequences, the glycosylation of the α- and γ-precursors, and the subsequent secretion of the 3 proteins. In the submaxillary gland, however, the mature forms of αNGF, γNGF and renin are composed of peptides of smaller size than those produced by the oocytes. These latter appear to lack specific proteases involved in the terminal processing of the submaxillary gland proteins