Purification and characterization of one of the forms of peptide hydrolases from guinea-pig small intestinal mucosa

J. Donlon; P. F. Fottrell

doi:10.1016/0005-2744(73)90426-9

Purification and characterization of one of the forms of peptide hydrolases from guinea-pig small intestinal mucosa

J. Donlon, P. F. Fottrell

Molecular Biosciences

University of Galway

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

20 Citations (Scopus)

Abstract

One of the forms of peptide hydrolases occurring in guinea-pig small intestinal mucosa was purified and characterized. The enzyme, formerly termed "α" peptidase, is an aminopeptidase with an apparent molecular weight of 300 000 daltons. It is activated by Mn²⁺ and is not inhibited by p-chloromercuribenzoate or diisopropylfluorophosphate. Kinetic parameters have been calculated to determine its substrate specificity. These results showed that this peptide hydrolase has a low order of specificity for dipeptides and tripeptides but preferentially hydrolysed peptides containing neutral or aromatic amino acid residues. The kinetics of hydrolysis of some substrates indicated that there may be two active sites on the enzyme molecule; one of these sites being Mn²⁺-dependent, the other Mn²⁺-independent. This aminopeptidase is compared to other well characterized aminopeptidases and its possible classification is also discussed.

Original language	English
Pages (from-to)	425-436
Number of pages	12
Journal	BBA - Enzymology
Volume	327
Issue number	2
DOIs	https://doi.org/10.1016/0005-2744(73)90426-9
Publication status	Published - 19 Dec 1973

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title = "Purification and characterization of one of the forms of peptide hydrolases from guinea-pig small intestinal mucosa",

abstract = "One of the forms of peptide hydrolases occurring in guinea-pig small intestinal mucosa was purified and characterized. The enzyme, formerly termed {"}α{"} peptidase, is an aminopeptidase with an apparent molecular weight of 300 000 daltons. It is activated by Mn2+ and is not inhibited by p-chloromercuribenzoate or diisopropylfluorophosphate. Kinetic parameters have been calculated to determine its substrate specificity. These results showed that this peptide hydrolase has a low order of specificity for dipeptides and tripeptides but preferentially hydrolysed peptides containing neutral or aromatic amino acid residues. The kinetics of hydrolysis of some substrates indicated that there may be two active sites on the enzyme molecule; one of these sites being Mn2+-dependent, the other Mn2+-independent. This aminopeptidase is compared to other well characterized aminopeptidases and its possible classification is also discussed.",

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T1 - Purification and characterization of one of the forms of peptide hydrolases from guinea-pig small intestinal mucosa

AU - Donlon, J.

AU - Fottrell, P. F.

PY - 1973/12/19

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N2 - One of the forms of peptide hydrolases occurring in guinea-pig small intestinal mucosa was purified and characterized. The enzyme, formerly termed "α" peptidase, is an aminopeptidase with an apparent molecular weight of 300 000 daltons. It is activated by Mn2+ and is not inhibited by p-chloromercuribenzoate or diisopropylfluorophosphate. Kinetic parameters have been calculated to determine its substrate specificity. These results showed that this peptide hydrolase has a low order of specificity for dipeptides and tripeptides but preferentially hydrolysed peptides containing neutral or aromatic amino acid residues. The kinetics of hydrolysis of some substrates indicated that there may be two active sites on the enzyme molecule; one of these sites being Mn2+-dependent, the other Mn2+-independent. This aminopeptidase is compared to other well characterized aminopeptidases and its possible classification is also discussed.

AB - One of the forms of peptide hydrolases occurring in guinea-pig small intestinal mucosa was purified and characterized. The enzyme, formerly termed "α" peptidase, is an aminopeptidase with an apparent molecular weight of 300 000 daltons. It is activated by Mn2+ and is not inhibited by p-chloromercuribenzoate or diisopropylfluorophosphate. Kinetic parameters have been calculated to determine its substrate specificity. These results showed that this peptide hydrolase has a low order of specificity for dipeptides and tripeptides but preferentially hydrolysed peptides containing neutral or aromatic amino acid residues. The kinetics of hydrolysis of some substrates indicated that there may be two active sites on the enzyme molecule; one of these sites being Mn2+-dependent, the other Mn2+-independent. This aminopeptidase is compared to other well characterized aminopeptidases and its possible classification is also discussed.

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Purification and characterization of one of the forms of peptide hydrolases from guinea-pig small intestinal mucosa

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