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- W965565915 abstract "The dipeptidyl aminopeptidases (DAP) are enzymes that catalyze the consecutive removal of dipeptide moieties from the unsubstituted NH2 termini of polypeptide chains. Four such enzymes are characterized and shown to have distinctive substrate specificities. Within this group, dipeptidyl aminopeptidase I (DAP I) exhibits the broadest substrate specificity. When DAP I is observed in bovine pituitary extracts, it is characterized as a sulfhydryl-dependent Ser-Tyr-β-naphthylamidase with an absolute or near-absolute chloride requirement and a pH 4 optimum. The purification serves as the basis for the preparation of DAP I. The practicability of using DAP I as a sequencing reagent is greatly enhanced by the relative ease with which a suitable preparation can be made. The broad substrate specificity of DAP I is first observed with β-corticotropin used as a substrate. DAP I activity has also been measured on Gly-Phe-NH2. An analysis of the specific bonds cleaved in polypeptide substrates revealed that DAP I can remove dipeptides having penultimate residues with both hydrophilic and hydrophobic side chains." @default.
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- W965565915 date "1972-01-01" @default.
- W965565915 modified "2023-09-26" @default.
- W965565915 title "[22] Preparation and specificity of dipeptidyl aminopeptidase I" @default.
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- W965565915 doi "https://doi.org/10.1016/s0076-6879(72)25024-8" @default.
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