Abstract
A preparation of hypertensin I was purified by countercurrent distribution and was shown to migrate as a single component in starch blocks at pH 9.3 and 4.2. It had an isoelectric point of 7.7. Quantitative analysis by ion exchange column chromatography showed eight amino acids in approximately unimolar proportion: aspartic, proline, valine, isoleucine, leucine, tyrosine, phenylalanine, and arginine. There were in addition two moles of histidine.
Keywords
AMINO ACIDS/determination
ANGIOTONIN
MeSH Terms
Amino Acids/analysis
Angiotensin Amide
Angiotensins
Arginine
Aspartic Acid
Glycine
Histidine
Isoleucine
Leucine
Phenylalanine
Proline
Serine
Tyrosine
Valine
Chemicals
Amino Acids
Angiotensins
Isoleucine
Aspartic Acid
Tyrosine
Serine
Phenylalanine
Histidine
Angiotensin Amide
Arginine
Proline
Leucine
Valine
Glycine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
SKEGGS L T
MARSH W H
KAHN J R
SHUMWAY N P
References (7)
7 references, click to expand
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PMID: 14946317
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The purification of hypertensin I.
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A method of assaying small amounts of hypertensin.
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PMID: 13045413
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The existence of two forms of hypertensin.
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Electrophoretic properties of oxytocin.
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