A novel method for purification of chicken cone visual pigments was established by use of a 3-[(3-cholamidopropyl)dimethylammonio]-1- propanesulfonate-phosphatidylcholine (CHAPS-PC) mixture. Outer segment membranes isolated from chicken retinas were extracted with 0.75% CHAPS supplemented with 1.0 mg/mL phosphatidylcholine (CHAPS-PC system). After the extract was diluted to 0.6% CHAPS, it was loaded on a concanavalin A-Sepharose column. Elution from the column with different concentrations of methyl alpha-mannoside yielded three fractions: the first was composed of chicken violet, blue, and red in roughly equal amounts, the second predominantly contained chicken red, and the third was rhodopsin with a small amount of chicken green, which was separated from rhodopsin by DEAE-Sepharose column chromatography. Since CHAPS has little absorbance at both ultraviolet and visible regions, we could demonstrate the absolute absorption spectra of chicken red (92%) and rhodopsin (greater than 96%) in these regions. The maximum of the difference spectrum between either chicken red or rhodopsin and its photoproduct (all-trans-retinal oxime plus opsin) was determined to be 571 or 503 nm, respectively. Although chicken green was contaminated with a small amount of rhodopsin having a similar spectral shape, the maximum of its difference spectrum was located at 508 nm by taking advantage of the difference in susceptibility against hydroxylamine between these pigments. Although chicken blue and chicken violet were minor pigments present in the first fraction from the concanavalin A column, their maxima in the difference spectra were determined to be at 455 and 425 nm, respectively, by a partial bleaching method.(ABSTRACT TRUNCATED AT 250 WORDS)

The primary structure of rhodopsin from the octopus Paroctopus depeini has heen determined by parallel analysis of the protein and corresponding cDNA. The amino acid sequence is most similar to the recently cloned Drosophila opsins. Similarities to bovine and human opsins are also evident. The transmembrane topology of octopus rhodopsin is discussed.

Iodopsin (a red-sensitive cone visual pigment) and rhodopsin (a rod pigment) were isolated from chicken retina. They were separately reconstituted into phosphatidylcholine liposomes and then mixed with rod transducin (Tot and TB~') purified from bovine retina, lodopsin enhanced, only when irradiated, the binding of GppNHp to T~t to a similar extent to irradiated rhodopsin. Furthermore, the binding of GppNHp to T~ in the presence of a photobleaching intermediate of iodopsin preferably required Tfly-2 rather than Tfly-l, which is very similar in profile to that in the presence of the intermediate of rhodopsin (J. Biol. Chem., in press). These results indicate that the binding domain for transducin in iodopsin should closely resemble that in rhodopsin.Cone visual pigment; Iodopsin; GTP-binding protein; Transducin; Rhodopsin; (Chicken retina)

The protein composition of human saliva depends on psycho-emotional state of individuals. Depression was accompanied by decrease of proteins of molecular masses ranging from 20 to 200 kD, whereas emotionally positive intellectual activity caused the opposite effect. It is suggested that human saliva may be used as an experimental model for the development of diagnostics of various psycho-physiological states.

T betagamma was shown to stimulate the hydrolysis and synthesis of PtdInsP2 in dark-adapted bovine retinal rod outer segments. In contrast, T alphaGDP blocked the effect of betagamma-transducin. It was also demonstrated that T betagamma was a stimulator of 32P incorporation into PtdInsP2 in ROS. These findings explain the modulating actions of GTP and light on PtdInsP2 hydrolysis and synthesis in ROS. The possible existence of cross-talk between the cGMP and phosphoinositide cascades in retinal rods was discussed.