The syntheses of the chain‐homologues of hypertensin, H · Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH, H · Asp(NH~2~)‐Arg‐Val‐Tyr‐Val‐His‐Pro · OH, and H · Asp(R)‐Arg‐Val‐Tyr‐Tyr‐Val‐His‐Pro‐Phe · OH (R −OH and −NH~2~), are described in detail. A system for the nomenclature of such analogues is proposed. The
Die sterische Einheitlichkeit des synthetischen Val5-Hypertensin II-Asp1-β-amids
✍ Scribed by B. Riniker; R. Schwyzer
- Publisher
- John Wiley and Sons
- Year
- 1961
- Tongue
- German
- Weight
- 678 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0018-019X
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✦ Synopsis
The enzymatic degradation of synthetic Val^5^‐Hypertensin II‐Asp^1^‐β‐amide with trypsin, chymotrypsin, pepsin, subtilisin, carboxypeptidase and leucineaminopeptidase is described, proving the optical purity of all amino‐acid residues (L‐configuration) except His^6^. The configuration of this amino‐acid has been confirmed by its quantitative destruction with L‐amino‐acid oxidase in hydrolysates.
📜 SIMILAR VOLUMES
The syntheses of H · Asp(NH~2~)‐Arg(NO~2~)‐Val‐Tyr‐Val‐His‐Pro‐Phe·OH (I) and of H · Asp(NH~2~)‐Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · NH~2~ (II), functional derivatives of hypertensin II (angiotensin II), are described. On total acid hydrolysis, nitroarginine and peptides thereof are degraded to arginine an
## Abstract The synthesis of two octapeptides, H · Asp(β‐NH~2~)‐Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH and H · Asp(β‐OH)‐Arg‐Val‐Tyr‐Val‐His‐Pro‐Phe · OH, is described in detail (preliminary communications see footnote 3). The products show a very strong hypertensive activity, and may be identical with t