The in vitro processing of the NGF precursors by the gamma-subunit of the 7S NGF complex.

The in vitro translation of the capped nerve growth factor (NGF) mRNA in wheat germ extracts produced a major 34 kDa NGF precursor with translation starting at the first methionine residue and a minor 29 kDa precursor with translation starting probably at the second methionine. Digestion with the gamma-subunit generated the 22 and 18 kDa intermediates as well as a very small amount of NGF indicating that the gamma-subunit is able to carry out all the processing steps in NGF biosynthesis. The digestion also produced a large amount of a peptide from the N-terminus of the NGF precursors. The discrepancy between the yield of this peptide and of mature NGF emphasizes that inappropriate formation or the lack of formation of disulfide bridges in the NGF precursors, resulting in rapid proteolysis, probably accounts for the low yield of the NGF peptide chains.