Purification of prosomatostatin-converting enzymes
- Robert B. Mackin(corresponding author),
- Bryan D. Noe,
- Joachim Spiess
- Max Planck Institute of Experimental Medicine,
- Salk Institute for Biological Studies,
- Emory University
Scholary Output:
Contribution to journal
Article
Peer-reviewSustainable Development Goals
- SDG 3 Good Health and Well
Abstract
The enzymes responsible for performing cleavage of propeptides at basic amino acids have proven difficult to characterize. Using the processing of anglerfish islet prosomatostatin (PSS) as a model system, we are pursuing the characterization of both a single basic amino acid-specific and a dibasic amino acid-specific converting enzyme. We describe here the model system and protein isolation methods that have allowed significant progress toward complete characterization of the somatostatin-generating propeptide converting enzymes (PCEs).
Publication Information
Output type
Scholary Output:
Contribution to journal
Article
Peer-reviewOriginal language
English (US)Pages from-to (Number of pages)
Pages 30-32 (3 pages)Journal (Volume, Issue Number)
Metabolism (Volume 39, Issue 9 SUPPL. 2)Publication milestones
- Published - 09/1990
Publication status
Published - 09/1990
ISSN
0026-0495Publication IDs
- Scopus: 0024992274
- PubMed: 1976216
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