Purification of prosomatostatin-converting enzymes

Robert B. Mackin; Bryan D. Noe; Joachim Spiess

doi:10.1016/0026-0495(90)90204-P

Purification of prosomatostatin-converting enzymes

Robert B. Mackin, Bryan D. Noe, Joachim Spiess

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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	https://doi.org/10.1016/0026-0495(90)90204-P
State	Published - Sep 1990
Externally published	Yes

All Science Journal Classification (ASJC) codes

Endocrinology, Diabetes and Metabolism
Endocrinology

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10.1016/0026-0495(90)90204-P

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title = "Purification of prosomatostatin-converting enzymes",

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).",

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