Phosphorylation of a peptide related to subunit c of the F0F1-ATPase/ATP synthase and relationship to permeability transition pore opening in mitochondria.

A phosphorylated polypeptide (ScIRP) from the inner membrane of rat liver mitochondria with an apparent molecular mass of 3.5 kDa was found to be immunoreactive with specific antibodies against subunit c of F0F1-ATPase/ATP synthase (Azarashvily, T. S.

Hofmeister effect in ion transport: reversible binding of halide anions to the roflamycoin channel.

We have studied the anion-dependent gating of roflamycoin ion channels using spectral analysis of noise in currents through multichannel planar lipid bilayers. We have found that in addition to low frequency current fluctuations that may be attributed to channel switching between open and closed conformations, roflamycoin channels exhibit a pronounced higher frequency noise indicating that the open channel conductance has substates with short lifetimes. This noise is well described by a Lorentzian spectrum component with a characteristic cutoff frequency that depends on the type of halide anions according to their position in the Hofmeister series.

On the protonophoric activity of oxazolomycin.

By the use of an artificial lipid membrane model we have shown that the antibiotic oxazolomycin (Streptomyces albus) is an effective protonophore at pH < 7.0 but conveys both protons and monovalent cations such as potassium at pH > 7.5 as a passive carrier.

Roflamycoin--a new channel-forming antibiotic.

Ion permeability of lipid bilayers was studied in the presence of a new antifungal pentaene antibiotic, roflamycoin, the structure of which differs considerably from that of the well-known polyene channel-former amphotericin B. Both of them, however, show the property of increasing the membrane permeability only in the case of sterol-containing membrane when added on both its sides. The conductance is strongly dependent on the concentration of the antibiotic in the solutions and of sterol in the membrane.

Isolation and properties of Ca2+-transporting glycoprotein and peptide from beef heart mitochondria.

The 40,000-dalton glycoprotein and 2000-dalton peptide inducing selective Ca2+-transport through bilayer lipid membranes were isolated from beef heart homogenate and mitochondria. Micromolar concentrations of these substances were found to increase the conductivity of membranes by 3-4 orders. Trans-membrane Ca2+ gradient induces an electric potential difference whose magnitude is close to the theoretical for ideal Ca2+ selectivity.