Structure of mouse submaxillary gland renin. Identification of two disulfide-linked polypeptide chains and the complete amino acid sequence of the light chain.
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Summary
Reduction and carboxymethylation of mouse submaxillary gland renin produced two polypeptide chains which were readily separated by gel filtration or sodium dodecyl sulfate-polyacrylamide gel electrophoresis and it was concluded that the heavy and light chains are linked by one disulfide bridge and that theheavy chain contains an intrachain disulfides bridge.
- Type
- article
- Published
- 1982-07-10
- Cited by
- 24
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1491816390
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19512742
Keywords
Disulfide bond, Chemistry, Sequence (biology), Submaxillary gland, Polypeptide chain
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- Renin processing studied by immunogold localization of prorenin and renin in granular juxtaglomerular cells in mice treated with enalapril
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- The storage form of renin in renin granules from rat kidney cortex.
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- Angiotensin-converting enzyme inhibitors: biochemical properties and biological actions.
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- Structure of the Mouse Submaxillary Gland Renin Precursor and a Model for Renin Processing: Arthur C. Corcoran Memorial Lecture
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