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. 1971 Oct;68(10):2417–2420. doi: 10.1073/pnas.68.10.2417

Nerve Growth Factor from Mouse Submaxillary Gland: Amino Acid Sequence

Ruth Hogue Angeletti *,*, Ralph A Bradshaw †,†
PMCID: PMC389434  PMID: 4944623

Abstract

The complete amino-acid sequence of the 2.5S nerve growth factor from male-mouse submaxillary glands has been determined. The unambiguous alignment of peptides derived from tryptic, chymotryptic, thermolytic, and peptic digestion of S-carboxymethyl-, S-aminoethyl-, and native growth factor indicates that the primary subunit is composed of 118 amino acids, with amino-terminal serine and carboxyl-terminal arginine. The molecular weight of this subunit, calculated from the primary sequence, is 13,259. Thus, the native protein, which is composed of two of the subunits, has a molecular weight of 26,518. These values, as well as the final amino-acid composition, are in excellent agreement with those determined by direct measurement with undigested growth factor. The alignment of the three disulfide bonds, determined from a combination of peptic and thermolytic digestions, is I-IV, II-V, and III-VI. The latter two pairs are located in a closed loop of 14 amino acids, by virtue of the fact that half-cystinyl residues V and VI are separated by only a single residue in the linear sequence. Assignment of the side-chain amides showed that 7 of 11 aspartic acid residues and 2 of 8 glutamic acid residues are present as amides. This distribution of charged residues is entirely consistent with the observed isoelectric point of 9.3.

Keywords: 2.5S protein, two subunits, disulfide bonds, enzymatic digestion

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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