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).
| Original language | English (US) |
|---|---|
| Pages (from-to) | 30-32 |
| Number of pages | 3 |
| Journal | Metabolism |
| Volume | 39 |
| Issue number | 9 SUPPL. 2 |
| DOIs | |
| State | Published - Sep 1990 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Endocrinology, Diabetes and Metabolism
- Endocrinology
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Cite this
Mackin, R. B., Noe, B. D., & Spiess, J. (1990). Purification of prosomatostatin-converting enzymes. Metabolism, 39(9 SUPPL. 2), 30-32. https://doi.org/10.1016/0026-0495(90)90204-P