Literature DB >> 3147705

The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A.

R D Wade1, G M Hass, S Kumar, K A Walsh, H Neurath.   

Abstract

The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A subunit I has been determined by automated Edman degradation of the cyanogen bromide fractions derived from the precursor protein. The activation peptide contains 94 amino acid residues in a unique sequence which precedes directly the amino-terminal alanine residue of carboxypeptidase A alpha. A notable feature of the activation peptide is the presence of acidic amino acid residues immediately preceding the site of activation. The amino acid sequence of the activation peptide of bovine pro-carboxypeptidase A shows extensive similarity to those of the corresponding porcine and rat enzymes.

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Year:  1988        PMID: 3147705     DOI: 10.1016/0300-9084(88)90178-2

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  1 in total

1.  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

  1 in total

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