NMR study of the possible interaction in solution of angiotensin II with a peptide encoded by angiotensin II complementary RNA
- Abbott Labs., Abbott Park, IL (USA)
- Univ. of Texas, Austin (USA)
The potential binding of angiotensin II (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) (AII) to a peptide encoded by its complementary RNA (Lys-Gly-Val-Asp-Val-Try-Ala-Val) (IIA) has been studied by monitoring the {sup 1}H NMR spectrum of IIA in aqueous phosphate or Tris{center dot}HCl buffer ({sup 2}H{sub 2}O) as it is titrated with AII. For molar ratios of AII/IIA ranging from 0.2 to 1.8, the NMR spectra are unchanged as compared to the spectra of the isolated peptides. Based on these findings, the K{sub d} for the putative biomolecular complex of the two peptides under these conditions is calculated to be >10{sup {minus}4} M. This result does not support the suggestion of Elton et al. that AII and IIA engage in high-affinity binding (K{sub d} {approx} 5 {times} 10 {sup {minus}8} M) with each other.
- OSTI ID:
- 6921072
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:24; ISSN 0027-8424; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
62 RADIOLOGY AND NUCLEAR MEDICINE
ANGIOTENSIN
AQUEOUS SOLUTIONS
BARYONS
BIOCHEMICAL REACTION KINETICS
CARDIOVASCULAR AGENTS
CHEMICAL REACTIONS
CROSS-LINKING
DISPERSIONS
DRUGS
ELEMENTARY PARTICLES
FERMIONS
GLOBULINS
HADRONS
HEAVY WATER
HYDROGEN COMPOUNDS
KINETICS
MAGNETIC RESONANCE
MESSENGER-RNA
MIXTURES
NUCLEAR MAGNETIC RESONANCE
NUCLEIC ACIDS
NUCLEONS
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PEPTIDES
POLYMERIZATION
PROTEINS
PROTONS
REACTION KINETICS
RESONANCE
RNA
SOLUTIONS
VASOCONSTRICTORS
WATER