Journal of Biological Chemistry · 1981 · 107 citations · 17 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProteomicsPeptide Bond ChemistryProtein DegradationProtein Sequence AnalysisProtein StructureProteolytic EnzymesProteolytic ProcessingCysteine ProteasesDisulfide ContributionsNerve Growth Factor SignalingProtease Cleavage SitesProtease Cleavage SpecificityProtease Substrate SpecificitySequence HomologySequence Homology Detection
The complete amino acid sequence of the gamma-subunit of mouse submaxillary gland 7 S nerve growth factor has been determined from analyses of the peptides generated by cyanogen bromide, trypsin, and chymotrypsin from the naturally occurring fragments. All peptides were sequenced automatically in a spinning-cup sequenator using Polybrene to minimize extractive losses by the solvents employed thoughout the degradation cycles. The gamma-subunit, a serine protease with arginine specificity, contains 233 amino acid residues and shares sequence homology with other proteases of this family. The five disulfide bonds of the gamma-subunit are a subset of the six disulfides present in bovine trypsin, as judged by the location of the half-cystine residues in the primary structure. An N-linked carbohydrate side chain is attached to Asn-78 in at least a majority of tee gamma-molecules.
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