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  • 1
    Electronic Resource
    Electronic Resource
    Preparations of Ψ-peptide bond and peptide-aldehyde inhibitors of atrial granule serine proteinase, a candidate processing enzyme of pro-atrial natriuretic factor (1995)
    Springer
    The protein journal 14 (1995), S. 431-440 
    Details
    ISSN: 1573-4943
    Keywords: ANF ; atrial natriuretic factors ; atrial granule serine proteinase ; peptide inhibitors ; peptide aldehydes ; processing enzymes ; pseudo-bond inhibitors ; serine proteinase ; Swern oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Pseudo-peptide bond inhibitors (ψ-bond inhibitors) and peptide-aldehyde inhibitors of atrial granule serine proteinase, the candidate processing enzyme of pro-atrial natrieuretic factor, are prepared in high yield and purity by novel synthetic routes. The ψ-bond compounds retain essential residues for enzyme binding, but place the enzyme inhibition site in the midst of the peptide sequence. Thus, Bz-APR-ψ-LR and Bz-APR-ψ-SLRR can be considered “readthrough inhibitors” of atrial granule serine proteinase. The most potent ψ-peptide, Bz-APR-ψ-SLRR (IC50=250 ΜM), is about fivefold less potent than the best peptide-aldehyde inhibitor (EACA-APR-CHO), and both the ψ-bond and peptide-aldehyde compounds are competitive, reversible inhibitors of the enzyme. The ψ-bond peptides containing two C-terminal Arg residues are three-to tenfold more potent than the analogous compounds containing only one C-terminal Arg residue, confirming the importance of both Arg residues in the enzyme processing recognition site. As expected, because of their moderate potencies, the ψ-peptides are not useful affinity ligands for purification of atrial granule serine proteinase, but both peptide aldehydes are effective affinity ligands [Damodaran and Harris (1995),J. Protein Chem., this issue].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888137
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  • 2
    Electronic Resource
    Electronic Resource
    N-terminal sequence analysis of atrial granule serine proteinase purified by affinity chromatography (1995)
    Springer
    The protein journal 14 (1995), S. 441-449 
    Details
    ISSN: 1573-4943
    Keywords: Affinity chromatography ; ANF ; atrial natriuretic factors ; atrial granule serine proteinase ; N-terminal sequence determination ; peptide inhibitors ; peptide aldehydes ; processing enzymes ; protein purification ; serine proteinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Atrial granule serine proteinase is considered the leading candidate endoproteolytic processing enzyme of pro-atrial natriuretic factor. Its cleavage specificity is directed toward a monobasic amino acid processing site, and as such, the atrial enzyme is distinguished from the family of prohormone convertases which act at dibasic amino acid processing sites. To delineate the molecular mechanisms which distinguish monobasic from dibasic amino acid-directed processing enzymes, pure atrial enzyme is needed for sequence determination leading to molecular cloning, and for preparation of antisera. An affinity chromatography purification scheme seemed a logical modification of our established procedures to yield suitable amounts of enzyme for further studies. Surprisingly, pseudo-peptide bond inhibitors of the atrial enzyme [Damodaran and Harris (1995),J. Protein Chem., this issue] formed ineffective affinity ligands, even though these compounds contain essential residues on either side of what would be the scissile bond in a peptide substrate. On the other hand, tripeptide aldehydes (based on the substrate recognition sequence of the atrial enzyme) linked to Sepharose formed effective affinity matrices, permitting purification of the enzyme in a single step from a subcellular fraction enriched for atrial granules and lysosomes. Hence, the enzyme was purified 2000-fold in 90% overall yield, and subjected to N-terminal sequence analysis through 26 residues. The sequence determined, XXPEAAGLPG[R, L]GNPVP[F, G]R[Q, I]XY[G, E]XR(N, A]V, indicates that the atrial enzyme is unique, showing little sequence homology to other proteins in the database.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888138
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