The determination of the amino acid sequence of nerve growth factor (NGF), prepared as the 2.5S derivative from mouse submandibular glands, has been initiated. Tryptic digestion of S-carboxymethyl- and S-aminoethyl-NGF, followed by purification and characterization of the resulting peptides, was performed. These peptides accounted for 87 residues in the NGF molecule but contained only 5 of the 6 half-cystinyl residues and were missing the amino-terminal fragment. Digestion of the S-carboxymethyl derivative with chymotrypsin yielded 19 peptides covering 108 unique residues. By combined Edman degradation and carboxypeptidase A and B digestion, 96 of the 108 residues, accounted for by peptides from the three separate digests were placed in sequence.
|Original language||English (US)|
|Number of pages||11|
|State||Published - 1973|
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