An Amphiphilic Form of Dipeptidyl Peptidase IV from Pig Small-Intestinal Brush-Border Membrane. Purification by Immunoadsorbent Chromatography and Some Properties
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چکیده
منابع مشابه
Cloning, purification, and enzymatic properties of dipeptidyl peptidase IV from the swine pathogen Streptococcus suis.
In this study, the dipeptidyl peptidase IV (DPP IV) of the swine pathogen Streptococcus suis was cloned, overexpressed in Escherichia coli, and characterized. The coding region comprises 2,268 nucleotides containing an open reading frame that codes for a 755-amino-acid protein with a calculated molecular mass of 85 kDa. The amino acid sequence contained the sequence Gly-X-Ser-X-X-Gly, which is ...
متن کاملPurification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography.
Membrane preparations from striatum of pig brain contain endopeptidase activity towards iodoinsulin B-chain. Only 50% of the hydrolysis of insulin B-chain is inhibitable by phosphoramidon, and DEAE-cellulose chromatography can resolve the phosphoramidon-sensitive and -insensitive activities. The former activity (now designated 'endopeptidase-24.11') is responsible for hydrolysis of [D-Ala2,Leu5...
متن کاملRat Intestinal Brush Border Membrane Peptidases
The properties of two purified peptidases derived from the intestinal brush border membrane of the rat have been investigated. The pH optima, heat stabilities, substrate specificities, and metal ion requirements of the two enzymes and the effects of inhibitors on their activities were nearly identical. The isoenzymes catalyzed the hydrolysis of a wide range of peptides containing from 2 to 8 am...
متن کاملIntestinal assimilation of a proline-containing tetrapeptide. Role of a brush border membrane postproline dipeptidyl aminopeptidase IV.
The mechanism of hydrolysis and absorption of a proline-containing tetrapeptide, Leu-Pro-Gly-Gly (10 mM) by rat intestine was examined in vivo by using jejunal perfusion methods. The peptide substrate and hydrolysis products were analyzed by use of an automated amino acid analyzer. Leucine, proline, and glycine were absorbed by the intestine at a significantly higher rate from the tetrapeptide ...
متن کاملDipeptidyl peptidase IV of Streptococcus anginosus: purification and characterization.
We found that N-unblocked nine p-nitroanilde derivatives of amino acids or peptides were hydrolyzed by the crude cell extracts of Streptococcus anginosus NCTC 10713. Then dipeptidyl peptidase IV was purified 323-fold by the procedures including ammonium sulfate concentration, anion exchange chromatography (twice), gel filtration (twice), hydrophobic interaction chromatography, and isoelectric f...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12628.x