Literature DB >> 109082

Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa.

C Doumeng, S Maroux.   

Abstract

Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa, was purified to homogeneity. The pure enzyme is a glycoprotein containing a very small amount of sugar. It is composed of only one subunit of 50,000 mol. wt. and possesses 1 zinc atom per molecule. Its specificity is primarily directed towards tripeptides with an N-terminal proline residue. However, the enzyme is also able to hydrolyse other tripeptides, except those with either a charged amino acid in the N-terminal position or a proline residue in the second position. The purified aminotripeptidase accounts for almost all the tripeptidase activity of the soluble fraction from intestinal mucosa.

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Year:  1979        PMID: 109082      PMCID: PMC1186443          DOI: 10.1042/bj1770801

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  21 in total

Review 1.  Intestinal absorption of peptides.

Authors:  D M Matthews
Journal:  Physiol Rev       Date:  1975-10       Impact factor: 37.312

2.  Topological studies on the hydrolases bound to the intestinal brush border membrane. I. Solubilization by papain and Triton X-100.

Authors:  D Louvard; S Maroux; C Vannier; P Desnuelle
Journal:  Biochim Biophys Acta       Date:  1975-01-28

3.  The thiobarbituric acid assay of sialic acids.

Authors:  L WARREN
Journal:  J Biol Chem       Date:  1959-08       Impact factor: 5.157

4.  EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS.

Authors:  D A YPHANTIS
Journal:  Biochemistry       Date:  1964-03       Impact factor: 3.162

5.  The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins.

Authors:  A M CRESTFIELD; S MOORE; W H STEIN
Journal:  J Biol Chem       Date:  1963-02       Impact factor: 5.157

6.  Amino acid and peptide absorption in man.

Authors:  D B Silk
Journal:  Ciba Found Symp       Date:  1977

7.  Histological localization of two dipeptidases in the pig small intestine and liver, using immunofluorescence.

Authors:  O Norén; E Dabelsteen; H Sjöström; L Josefsson
Journal:  Gastroenterology       Date:  1977-01       Impact factor: 22.682

8.  Disposition of the major proteins in the isolated erythrocyte membrane. Proteolytic dissection.

Authors:  T L Steck; G Fairbanks; D F Wallach
Journal:  Biochemistry       Date:  1971-06-22       Impact factor: 3.162

9.  Substrate specificity of a highly active dipeptidase purified from monkey small intestine.

Authors:  M Das; A N Radhakrishnan
Journal:  Biochem J       Date:  1972-06       Impact factor: 3.857

10.  Post-proline cleaving enzyme. Purification of this endopeptidase by affinity chromatography.

Authors:  M Koida; R Walter
Journal:  J Biol Chem       Date:  1976-12-10       Impact factor: 5.157

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  3 in total

1.  Purification and characterization of tripeptide aminopeptidase from bovine dental follicles.

Authors:  B Y Hiraoka; M Harada
Journal:  Mol Cell Biochem       Date:  1993-12-08       Impact factor: 3.396

Review 2.  Structural specificity of mucosal-cell transport and metabolism of peptide drugs: implication for oral peptide drug delivery.

Authors:  J P Bai; G L Amidon
Journal:  Pharm Res       Date:  1992-08       Impact factor: 4.200

Review 3.  Proline specific endo- and exopeptidases.

Authors:  R Walter; W H Simmons; T Yoshimoto
Journal:  Mol Cell Biochem       Date:  1980-04-18       Impact factor: 3.396

  3 in total

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