Bimolecular (black) lipid membranes: study of lipid-protein interactions.

An experimental method has been devised for the study of the inter-action of bimolecular (black) lipid membrane and protein in which 8-anilino-1-naphthalenesulfonic acid is used as a fluorescent probe. The presence of phospho-lipid in the membrane is necessary for the enhanced fluorescence.

Photochemical yields in ribonuclease and oxidized glutathione irradiated at different wavelengths in the ultraviolet.

The quantum yields for the disruption of various amino acids in glutathione and ribonuclease by 229, 254, 265, and 280 nm UV photons have been determined. The results of the measurements on the destruction of tyrosine and histidine and the loss of enzymic function in RNAse and the disruption of cystine in both compounds lead to the following conclusions: (a) The photodestruction of some and perhaps many constituent amino acid residues does not cause RNAse inactivation. (b) Contrary to the basic premise of proposals made by other authors, the photochemical yields of constituent residues in a protein are not the same as that for the same amino acids in solution alone-the difference is a function of the exciting wavelength. Further, the extent of histidine destruction varies by a large factor among three proteins. (c) Consistent with previous predictions, the present results show that photons absorbed in the aromatic residues of RNAse cause the disruption of cystines elsewhere in the enzyme. (d) Although cystine disruption appears to be the most prevalent mode of RNAse inactivation by photons of the four wavelengths studied, some of the minor mechanisms leading to loss of enzymic function may vary with the UV energy.