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- W1428989872 abstract "Dipeptidases hydrolyze only a-L-dipeptides with free amino and carboxyl groups. The exception observed is exceedingly slow hydrolysis of dipeptides with methyl-substituted amino groups. The products of the reaction are the constituent amino acids of the dipeptides. Dipeptides with amino groups blocked by a benzoyl or carbobenzoxy group, dipeptide or amino acid amides, dipeptides with the amino group in the fl-position, and tripeptides, are not hydrolyzed. This chapter elaborates on two assay methods performed to establish this observation. In method A the amino acids resulting from the hydrolyses of dipeptides are estimated by a photometric ninhydrin method that is a modification of that of Matheson and Tattrie. In method B the difference in absorbance in the low ultraviolet between dipeptides and their constituent amino acids is observed. This method is used for kinetic studies in which the concentration of a variety of dipeptide substrates was varied from 50 down to 0.8 mM. The chapter details on the procedures followed on both the assays. It also discusses the purification procedure, the purity and physical properties of dipeptidase, its pH dependence and inhibitors." @default.
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- W1428989872 date "1976-01-01" @default.
- W1428989872 modified "2023-09-24" @default.
- W1428989872 title "[30] A Dipeptidase from Escherichia coli B" @default.
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- W1428989872 doi "https://doi.org/10.1016/s0076-6879(76)45033-4" @default.
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