On the mechanism of action of phospholipase A
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This article is published in Biochemical Journal.The article was published on 1963-09-01 and is currently open access. It has received 149 citations till now. The article focuses on the topics: Phospholipase A & Phospholipase.read more
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Journal ArticleDOI
Diffusion of Univalent Ions Across the Lamellae of Swollen Phospholipids
TL;DR: It is found that as the surface charge of the lipid lamellae is increased, the amount of cation per μmle of lipid increases, and the phospholipid liquid crystalline structures appear to “bind” or “capture” cations.
Journal ArticleDOI
The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. VI. Evidence for a role of membrane lipids.
TL;DR: Plasma membranes prepared from rat livers treated with digitonin or phospholipase A under conditions which result in substantial loss of glucagon- Stimulated adenyl cyclase activity but no loss of fluoride-stimulated activity are thought to reflect extensive modification of the structures responsible for hormone sensitivity without destruction of the catalytic component of the adeny cyclase system.
Journal ArticleDOI
The action of steroids and streptolysin S on the permeability of phospholipid structures to cations.
TL;DR: These studies support the concept that aqueous suspensions of phospholipids constitute valuable model systems, and suggest that the membrane-action of biologically active steroids result from their direct interaction with lipid, independent of polysaccharide, protein or active cell metabolism.
Journal ArticleDOI
Cyclodepsipeptides as chemical tools for studying ionic transport through membranes
M. M. Shemyakin,Yu.A. Ovchinnikov,Vadim T. Ivanov,V.K. Antonov,E. I. Vinogradova,A.M. Shkrob,G. G. Malenkov,A. V. Evstratov,I. A. Laine,E. I. Melnik,I. D. Ryabova +10 more
TL;DR: The studies have clearly shown the feasibility of using cyclodepsipeptides with predetermined structural and conformational parameters as chemical tools for membrane studies and it is suggested that the principle of conformation-dependent cation binding through iondipole interactions may possibly lie at the basis of the mode of action of systems governing the natural ion permeability in biological membranes.
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