Literature DB >> 1417781

cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1.

L Catasús1, V Villegas, R Pascual, F X Avilés, C Wicker-Planquart, A Puigserver.   

Abstract

Using polyclonal antibodies raised against human pancreatic procarboxypeptidases, a full-length cDNA coding for an A-type proenzyme was isolated from a lambda gt11 human pancreatic library. This cDNA contains standard 3' and 5' flanking regions, a poly(A)+ tail and a central region of 1260 nucleotides coding for a protein of 419 amino acids. On the basis of sequence comparisons, the human protein was classified as a procarboxypeptidase A1 which is very similar to the previously described A1 forms from rat and bovine pancreatic glands. The presence of the amino acid sequences assumed to be of importance for the zymogen inhibition by its activation segment, primarily on the basis of the recently reported crystal structure of the B form, further supports the proposed classification.

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Year:  1992        PMID: 1417781      PMCID: PMC1133158          DOI: 10.1042/bj2870299

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


  18 in total

1.  Purification and properties of five different forms of human procarboxypeptidases.

Authors:  R Pascual; F J Burgos; M Salva; F Soriano; E Mendez; F X Aviles
Journal:  Eur J Biochem       Date:  1989-02-15

2.  Identification of the amino acid replacements characterizing the allotypic forms of bovine carboxypeptidase A.

Authors:  P H Pétra; R A Bradshaw; K A Walsh; H Neurath
Journal:  Biochemistry       Date:  1969-07       Impact factor: 3.162

3.  The amino acid sequence of bovine carboxypeptidase A.

Authors:  R A Bradshaw; L H Ericsson; K A Walsh; H Neurath
Journal:  Proc Natl Acad Sci U S A       Date:  1969-08       Impact factor: 11.205

Review 4.  Compilation of published signal sequences.

Authors:  M E Watson
Journal:  Nucleic Acids Res       Date:  1984-07-11       Impact factor: 16.971

5.  Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes.

Authors:  M Kozak
Journal:  Nucleic Acids Res       Date:  1981-10-24       Impact factor: 16.971

6.  Structural characterization of the rat carboxypeptidase A1 and B genes. Comparative analysis of the rat carboxypeptidase gene family.

Authors:  E Clauser; S J Gardell; C S Craik; R J MacDonald; W J Rutter
Journal:  J Biol Chem       Date:  1988-11-25       Impact factor: 5.157

7.  The tryptic activation pathway of monomeric procarboxypeptidase A.

Authors:  J Vendrell; C M Cuchillo; F X Avilés
Journal:  J Biol Chem       Date:  1990-04-25       Impact factor: 5.157

8.  DNA sequencing with chain-terminating inhibitors.

Authors:  F Sanger; S Nicklen; A R Coulson
Journal:  Proc Natl Acad Sci U S A       Date:  1977-12       Impact factor: 11.205

9.  Rat preprocarboxypeptidase A: cDNA sequence and preliminary characterization of the gene.

Authors:  C Quinto; M Quiroga; W F Swain; W C Nikovits; D N Standring; R L Pictet; P Valenzuela; W J Rutter
Journal:  Proc Natl Acad Sci U S A       Date:  1982-01       Impact factor: 11.205

10.  Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity.

Authors:  M Coll; A Guasch; F X Avilés; R Huber
Journal:  EMBO J       Date:  1991-01       Impact factor: 11.598

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  2 in total

1.  Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.

Authors:  Richárd Szmola; Melinda Bence; Andrea Carpentieri; András Szabó; Catherine E Costello; John Samuelson; Miklós Sahin-Tóth
Journal:  J Biol Chem       Date:  2010-11-22       Impact factor: 5.157

2.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1992-12-25       Impact factor: 16.971

  2 in total

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