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Similarities of the substrate cleavage catalyzed by proline specific endopeptidase and dipeptidyl peptidase IV

Weidhase, R. and Welker, P. and Neubert, K. and Dove, Stefan and Yoshimoto, T. and Tsuru, D. and Barth, A. (1984) Similarities of the substrate cleavage catalyzed by proline specific endopeptidase and dipeptidyl peptidase IV. Pharmazie 39 (12), pp. 835-837.

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Other URL: http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=search&db=pubmed&doptcmdl=Abstract&term=0031-7144%20AND%201984[Publication%20Date]%20AND%2039[Volume]%20AND%20835[Page%20Number]


Abstract

Sixteen substrates of the type succinyl-Ala-Ala-pX-anilide and succinyl-Ala-Pro-pX anilide having different substituents (X) in p-position of the aryl residue were synthesized and characterized. The influence of electronic as well as hydrophobic substituent consts., s and p, on the hydrolysis of substrates catalyzed by proline-specific endopeptidase (PSE) was investigated. In the Hansch ...

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Item Type:Article
Date:1984
Institutions:Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer)
Identification Number:
ValueType
1985:145207Other
Subjects:500 Science > 540 Chemistry & allied sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:No
Owner: Prof. Dr. Stefan Dove
Deposited On:14 Jan 2009 15:12
Last Modified:05 Aug 2009 13:50
Item ID:5469
Owner Only: item control page
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