Literature DB >> 4052013

Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases A.

M Vilanova, J Vendrell, M T López, C M Cuchillo, F X Avilés.   

Abstract

A method is reported for the preparative isolation of the two forms of pro-(carboxypeptidase A) from pig pancreas: the monomer and the binary complex with pro-(proteinase E). This method, which is mainly based on chromatography on DEAE-Sepharose at pH 5.7, allows these proenzymes to be prepared more quickly and in safer conditions than with other reported methods. Undegraded and homogeneous carboxypeptidase A1 and A2 species (peptidyl-L-amino acid hydrolase, EC 3.4.17.1), in monomeric forms with high specific activity, are also obtained in high yield by controlled trypsin activation of either of the pro-(carboxypeptidases A) followed by chromatography on DEAE-Sepharose at pH 5.8 under dissociating conditions (7 M-urea).

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Year:  1985        PMID: 4052013      PMCID: PMC1145102          DOI: 10.1042/bj2290605

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


  16 in total

1.  Two-dimensional gel analysis of soluble proteins. Charaterization of guinea pig exocrine pancreatic proteins.

Authors:  G A Scheele
Journal:  J Biol Chem       Date:  1975-07-25       Impact factor: 5.157

2.  CHYMOTRYPSIN C. I. ISOLATION OF THE ZYMOGEN AND THE ACTIVE ENZYME: PRELIMINARY STRUCTURE AND SPECIFICITY STUDIES.

Authors:  J E FOLK; E W SCHIRMER
Journal:  J Biol Chem       Date:  1965-01       Impact factor: 5.157

3.  Electrophoretic analysis of the unfolding of proteins by urea.

Authors:  T E Creighton
Journal:  J Mol Biol       Date:  1979-04-05       Impact factor: 5.469

4.  On the two anionic chymotrypsinogens of porcine pancreas.

Authors:  D Gratecos; O Guy; M Rovery; P Desnuelle
Journal:  Biochim Biophys Acta       Date:  1969-02-04

5.  Isolation and re-association of the subunits from the pro-(carboxypeptidase A)-pro-(proteinase E) binary complex from pgi pancreas.

Authors:  J Vendrell; F X Aviles; B San Segundo; C M Cuchillo
Journal:  Biochem J       Date:  1982-08-01       Impact factor: 3.857

6.  Comparison between the monomeric and binary-complex forms of procarboxypeptidase A from whole pig pancreas.

Authors:  M C Martínez; F X Avilés; B Sansegundo; C M Cuchillo
Journal:  Biochem J       Date:  1981-07-01       Impact factor: 3.857

7.  The severed activation segment of porcine pancreatic procarboxypeptidase A is a powerful inhibitor of the active enzyme. Isolation and characterisation of the activation peptide.

Authors:  B S Segundo; M C Martínez; M Vilanova; C M Cuchillo; F X Avilés
Journal:  Biochim Biophys Acta       Date:  1982-09-22

8.  Crystallization and properties of carboxypeptidase A gamma from porcine pancreas.

Authors:  A Koide; M Yoshizawa; K Kurachi
Journal:  Eur J Biochem       Date:  1981-07

9.  Identification of a binary complex of procarboxypeptidase A and a precursor of protease E in porcine pancreatic secretion.

Authors:  R Kobayashi; Y Kobayashi; C H Hirs
Journal:  J Biol Chem       Date:  1978-08-10       Impact factor: 5.157

10.  The specificity of porcine pancreatic protease E.

Authors:  R Kobayashi; Y Kobayashi; C H Hirs
Journal:  J Biol Chem       Date:  1981-03-10       Impact factor: 5.157

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  4 in total

1.  The activation pathway of procarboxypeptidase B from porcine pancreas: participation of the active enzyme in the proteolytic processing.

Authors:  V Villegas; J Vendrell; X Avilés
Journal:  Protein Sci       Date:  1995-09       Impact factor: 6.725

2.  1H-n.m.r. studies of the isolated activation segment from pig procarboxypeptidase A.

Authors:  J Vendrell; F X Avilés; M Vilanova; C H Turner; C Crane-Robinson
Journal:  Biochem J       Date:  1990-04-01       Impact factor: 3.857

3.  Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A.

Authors:  M Vilanova; J Vendrell; C M Cuchillo; F X Avilés
Journal:  Biochem J       Date:  1988-05-01       Impact factor: 3.857

4.  The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.

Authors:  J Vendrell; M Billeter; G Wider; F X Avilés; K Wüthrich
Journal:  EMBO J       Date:  1991-01       Impact factor: 11.598

  4 in total

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