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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1994-3-23
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pubmed:abstractText |
The N-acylpeptide hydrolase from porcine intestinal mucosa was 2000-fold purified by a five-step procedure. The resulting protein (about 300 kDa) is composed of four apparently identical N-acylated polypeptide chains. The enzyme activity was found to be equally distributed along the crypt-villus axis in the intestine and was characterized as a cytosolic protein. Besides the ability of porcine intestinal APH to cleave the first peptide bond in N-protected peptides (Km: 0.8 mM), it is worth stressing that the enzyme was also found to efficiently catalyze the hydrolysis of the isopeptide bond in N-epsilon-Ac-L-Met-L-Lys (Km: 0.7-1.1 mM). It is suggested that N-acylpeptide hydrolase might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0300-9084
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
891-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7906149-Alkaline Phosphatase,
pubmed-meshheading:7906149-Amino Acid Sequence,
pubmed-meshheading:7906149-Aminopeptidases,
pubmed-meshheading:7906149-Animals,
pubmed-meshheading:7906149-Antigens, CD13,
pubmed-meshheading:7906149-Chromatography, High Pressure Liquid,
pubmed-meshheading:7906149-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7906149-Hydrolysis,
pubmed-meshheading:7906149-Intestinal Mucosa,
pubmed-meshheading:7906149-Kinetics,
pubmed-meshheading:7906149-Male,
pubmed-meshheading:7906149-Molecular Sequence Data,
pubmed-meshheading:7906149-Molecular Weight,
pubmed-meshheading:7906149-Oligopeptides,
pubmed-meshheading:7906149-Peptide Hydrolases,
pubmed-meshheading:7906149-Rats,
pubmed-meshheading:7906149-Rats, Wistar,
pubmed-meshheading:7906149-Swine,
pubmed-meshheading:7906149-Tissue Distribution
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pubmed:year |
1993
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pubmed:articleTitle |
The N-acylpeptide hydrolase from porcine intestine: isolation, subcellular localization and comparative hydrolysis of peptide and isopeptide bonds.
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pubmed:affiliation |
Laboratoire de Biochimie et Biologie de la Nutrition, CNRS-ERS 25, Faculté des Sciences et Techniques St-Jérôme, Marseille, France.
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pubmed:publicationType |
Journal Article
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