Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues.
Asp-N, an endoproteinase specific for cleavage of protein or polypeptide bonds N-terminal to aspartate or cysteic acid residues, has been shown to possess a similar affinity for certain glutamate residues. Of 18 glutamate residues present in 2 cyanogen bromide fragments of apolipoprotein A-I, 5 residues were cleaved at rates comparable to that of cleavage at the 12 internal aspartate residues present in these polypeptides (all of which were cleaved). Cleavage of these 5 glutamate residues was obtained under standard enzyme digestion conditions, and the identities of all peptides obtained by Asp-N digestion were determined by amino acid sequencing of peaks obtained from reversed-phase high performance liquid chromatography.
Tetaz
T
T
Baker Medical Research Institute, Prahran, Victoria, Australia.
Morrison
J R
JR
Andreou
J
J
Fidge
N H
NH
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D016632:Apolipoprotein A-I; D001054:Apolipoproteins A / Q000378:metabolism; D001224:Aspartic Acid; D002851:Chromatography, High Pressure Liquid; D003544:Cysteic Acid; D010450:Endopeptidases / Q000378:metabolism*; D005971:Glutamates; D018698:Glutamic Acid; D006801:Humans; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*; D013379:Substrate Specificity
D000596:Amino Acids; D016632:Apolipoprotein A-I; D001054:Apolipoproteins A; D005971:Glutamates; D010446:Peptide Fragments; D001224:Aspartic Acid; D018698:Glutamic Acid; D003544:Cysteic Acid; D010450:Endopeptidases; D008666:Metalloendopeptidases; C058921:endoproteinase Asp-N