PubMed Health⌕ Search

Biomedical subjects

F Tokunaga

Publications and source records attributed to F Tokunaga.

At least 163 records · Page 9Linked to original sources
PubMed1978

Circular dichroism of squid rhodopsin and its intermediates.

Circular dichroism (CD) and absorption spectra of squid (Todarodes pacificus) rhodopsin, isorhodopsin and the intermediates was measured at low temperatures. Squid rhodopsin has positive CD bands at wavelengths corresponding the alpha- and beta-absorption bands at liquid nitrogen temperature (CD maxima: 485 nm at alpha-band and 348 nm at beta-band) as well as at room temperature (CD maxima: 474 nm at alpha-band and 347 nm at beta-band). The rotational strength of the alpha-band has a molecular ellipticity about twice that of cattle rhodopsin. The CD spectrum of bathorhodopsin displays a negative peak at 532 nm, the rotational strength of which has an absolute value slightly larger than that of rhodopsin. The reversal in sign at alpha-band of the CD spectrum may indicate that the isomerization of retinal chromophore from twisted 11-cis form to twisted 11-trans form has occurred in the process of conversion from rhodopsin to bathorhodopsin. Lumirhodopsin has a small negative CD band at 490 nm, the maximum of which lies at 25 nm shorter wavelengths than the absorption maximum (515 nm), and a large positive CD band near 290 nm, which is not observed in rhodopsin and the other intermediates. This band may de derived from a conformational change of the opsin. In the process of changing from lumirhodopsin to LM-rhodopsin, The CD bands at visible and near ultraviolet regions disappear. Both alkaline and acid metarhodopsins have no CD bands at visible and near ultraviolet regions.

Animals↗
PubMed1977

Synthetic pigment analogues of the purple membrane protein.

Nonphysiological analogues of retinal have been shown to form pigments in reactions with the apoprotein of the purple membrane of Halobacterium halobium. Both the all-trans and 13-cis isomers of a retinal analogue, having an elongated chain with an extra double bond, formed pigments. Unlike the native all-trans and 13-cis retinal1-based pigments, the new pigments were not interconvertible with each other and were unstable against hydroxylamine. When incorporated into phospholipid vesicles, they showed no proton pumping activity upon illumination. The ability of the extended-length retinal to form pigments contrasts with its nonreactivity with opsin (apoprotein of rhodopsin), suggesting a less stringent binding site for the purple membrane chromophore. All-trans retinal2 also combined with bleached purple membrane to form a blue pigment absorbing at ca. 590 nm. Like the native purple membrane, the blu membrane showed proton pumping activity upon illumination in phospholipid vesicles.

Apoproteins↗
PubMed1975

Accessibility of the iodopsin chromophore.

Iodopsin can replace its chromophore (11-cis retinal) by added 9-cis retinal, resulting in the formation of isoiodopsin. NaBH4 bleaches iodopsin in the dark. In a relatively low concentration of digitonin, the scotopsin (the protein moiety of chicken rhodopsin) removes 11-cis retinal from iodopsin in the dark. These facts suggest that the linkage of the chromophore to opsin in the iodopsin molecule (presumably a Schiff-base linkage) is accessible to these reagents, which is different from the situation in rhodopsin.

Alcohol Oxidoreductases↗
PubMed1975

Inhibitory effect of U.V. -irradiation on the formation of twisted circular lambda DNA.

Ultra-violet irradiation of lambda phage results in an inhibition of conversion of lambda DNA in host cells from the initial linear form to twisted circular form. The formation of open circular lambda DNA in vitro (formation of Hershey's circle) was quite resistant to the irradiation. The occurrence of denaturation of ultraviolet irradiation was detected in lambda DNA.

Centrifugation, Zonal↗