[Dipeptidyl peptidase IV. Purification for use in peptide sequencing]
- PMID: 2859040
[Dipeptidyl peptidase IV. Purification for use in peptide sequencing]
Abstract
Isolation and purification of dipeptidyl peptidase IV from pig kidney are described. The specific activity of the enzyme is 24.9 U/mg protein. Chromatography on Gly-Pro-AH-Sepharose is the most important procedure for the separation from other enzyme activities. The enzyme preparation is free of aminopeptidase, dipeptidase and prolyl endopeptidase activity; it can be used for peptide-sequence analysis.
Similar articles
-
A simple method for the purification of dipeptidyl aminopeptidase IV from porcine kidney using HPLC.Biomed Chromatogr. 1986 Aug;1(4):147-50. doi: 10.1002/bmc.1130010403. Biomed Chromatogr. 1986. PMID: 2906548
-
Preparative purification of dipeptidyl peptidase IV.Prep Biochem. 1991;21(2-3):141-50. doi: 10.1080/10826069108018009. Prep Biochem. 1991. PMID: 1686804
-
Purification and properties of human placental dipeptidyl peptidase IV.Nihon Sanka Fujinka Gakkai Zasshi. 1985 May;37(5):769-75. Nihon Sanka Fujinka Gakkai Zasshi. 1985. PMID: 2860191
-
Peptidomics of the prolyl peptidases.AAPS J. 2010 Dec;12(4):483-91. doi: 10.1208/s12248-010-9208-y. Epub 2010 Jun 16. AAPS J. 2010. PMID: 20552307 Free PMC article. Review.
-
Research Progress on Dipeptidyl Peptidase Family: Structure, Function and Xenobiotic Metabolism.Curr Med Chem. 2022;29(12):2167-2188. doi: 10.2174/0929867328666210915103431. Curr Med Chem. 2022. PMID: 34525910 Review.
Cited by
-
Purification and Partial Characterization of a Prolyl-Dipeptidyl Aminopeptidase from Lactobacillus helveticus CNRZ 32.Appl Environ Microbiol. 1990 Feb;56(2):381-8. doi: 10.1128/aem.56.2.381-388.1990. Appl Environ Microbiol. 1990. PMID: 16348113 Free PMC article.