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PMID: 13463253 Published · ppublish English Journal Article

The preparation, purification, and amino acid sequence of a polypeptide renin substrate.

The Journal of experimental medicine ·Vol. 106 ·No. 3 ·1957-09-01 ·Pages 439-53

SKEGGS LT, KAHN JR, LENTZ K, SHUMWAY NP

Abstract

A purified preparation of a polypeptide renin substrate prepared by tryptic degradation of the protein renin substrate has been analyzed by the fluorodinitrobenzene method and after degradation with renin, carboxypeptidase, and phenylisothiocyanate, has been found to possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser. The first 10 of these amino acids constitutes hypertensin I which is released by cleavage of the leucyl-leucine bond by renin. The remaining 4 amino acids, leu, val, tyr, ser, apparently link hypertensin I to the protein renin substrate.

Keywords
PEPTIDES PROTEASES
MeSH Terms
Amino Acid Sequence Amino Acids Angiotensinogen Dipeptides Endopeptidases Peptide Hydrolases Peptides
Chemicals
Amino Acids Dipeptides Peptides arginylvaline valyltyrosine Angiotensinogen histidylproline leucylleucine histidylleucine Endopeptidases Peptide Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
SKEGGS L T
KAHN J R
LENTZ K
SHUMWAY N P
References (16)
16 references, click to expand
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
Published
1957-09-01
Pages
439-53
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2136772
Subset
OM
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