PMID: 38854Aug 22, 1979

Angiotensin and bradykinin interactions with phospholipids

Biochimica Et Biophysica Acta
M E Elliott, T L Goodfriend

Abstract

Reversible interactions were demonstrated between some phospholipids and some polypeptides related to angiotensin and bradykinin. The extent of the interaction was dependent on the structures of the lipid and peptide. The naturally occurring compounds that interacted most avidly were cardiolipin and (des-Asp1)-angiotensins. The apparent dissociation constant of this complex in chloroform was 10(-5) M. The complex contained more than one cardiolipin molecule/molecule of peptide. Kinins interacted most strongly with lecithin. The phospholipids altered the chromatographic behavior of radioiodinated derivatives of the polypeptides, and solubilized radioactive and unlabeled polypeptides in chloroform. In aqueous media, cardiolipin suspensions preferentially bound (des-Asp1)-angiotensin II, and inhibited its binding by antibody. The interactions were sensitive to pH and cations in the aqueous phase, and were reversed by some reagents added to the organic phase. These interactions have direct implications for binding reactions of peptides in vitro, and may bear upon the actions of the hormones in vivo.

References

Mar 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·B R MullinR O Brady
Jun 11, 1971·Science·A L Robertson, P A Khairallah
Jul 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·J T SparrowJ D Morrisett

Related Concepts

Angiotensin II, Val(5)-
Angiotensin III
Antigen-Antibody Reactions
Bradykinin, (3-D-Pro)-Isomer
Diphosphatidylglycerols
Cations, Divalent
Hydrogen-Ion Concentration
Kallidin, (D)-Isomer
Phospholipids
Plasma Protein Binding Capacity

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