A tryptic digestion fragment of nerve growth factor with nerve growth promoting activity

Autor: R. Revoltella, D. Mercanti, R. Butler
Rok vydání: 1977
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - General Subjects. 496:412-419
ISSN: 0304-4165
DOI: 10.1016/0304-4165(77)90323-3
Popis: A peptide, isolated from the acid-insoluble portion of a tryptic digest of cyanogen bromide cleaved nerve growth factor, favors life maintenance of sensory target cells and promotes rapid neurite outgrowth from 7-day-old chick embryo sensory ganglia. The fragment has been identified as a 30 amino acid peptide consisting of two linear oligipeptides linked by a disulphide bridge and corresponding to residues 10–25 and 75–88 of the amino acid sequence of nerve growth factor. On a molar basis the fragment is about 100 times more effective than intact nerve growth factor. Other peptides isolated from the digest are biologically inactive.
Databáze: OpenAIRE