𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Determination of leucine aminopeptidase using phenylalanyl-3-thia-phenylalanine as substrate

✍ Scribed by Se Young Hwang; William D. Kingsbury; Norman M. Hall; Dalia R. Jakas; George L. Dunn; Charles Gilvarg

Publisher
Elsevier Science
Year
1986
Tongue
English
Weight
503 KB
Volume
154
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis

The peptide mimetic L-phenylalanyl-L-3-thiaphenylalanine has been shown to facilitate a sensitive and simple determination of Ieucine aminopeptidase. A calorimetric assay, employing Ellman's reagent to detect the thiophenol released upon hydrolysis of the dipeptide, has been developed. Under the experimental conditions employed the substrate has a k;, of 0.054 mM and a k,, of 5800 min-' and can distinguish sharply between leucine aminopeptidase and aminopeptidase M.

πŸ“œ SIMILAR VOLUMES

Determination of carboxypeptidase A usin
Determination of carboxypeptidase A using N-acetyl-phenylalanyl-3-thiaphenylalanine as substrate: Application to a direct serum assay
✍ Karen S. Brown; William D. Kingsbury; Norman M. Hall; George L. Dunn; Charles Gi πŸ“‚ Article πŸ“… 1987 πŸ› Elsevier Science 🌐 English βš– 507 KB

## N-Acetyl-L-phenylalanyl-L-34hiaphenylalanine has been shown to be a substrate for carboxypeptidase A. Hydrolysis of the compound obeys Michaelis-Menten kinetics with a KM of 0.22 mM and a k,,, of 6720 min-' at 22Β°C. A calorimetric assay, employing Ellman's reagent to detect the thiophenol relea