[The use of triplet-sensitized photochromism phenomenon for the study of dynamic interaction of membrane proteins].
Possibility of registration of protein interactions in the membranes was demonstrated. The membrane preparation of Na+, K+ ATPase was used in the investigations. The Na+, K+ ATPase was bound with 4-acetoamido-4'-isothiocyanatostilbene-2,2' disullfonic acid (SITS) and erythrosinisothiocyanate (ERITC). The label/Na+,K+ATPase (M/M) ratio was equal to 1:1 for SITS and changed from 1:1 to 1:5 for ERITC. The cis-trans isomerization of SITS was initiated by triplet-triplet energy transfer from light excited ERITC to SITS. The kinetics of isomerization was recorded by the SITS fluorescence measurements. The rate constant of triplet-triplet energy transfer (kT) from ERITC to cis isomer of SITS, (3 divided by 7) X 10(3) M-1 s-1 was determined at 25 degrees C. The kT value of the energy transfer between loose molecules of erythrosine and SITS in buffer solution equaled to 7 X 10(7) M-1 s-1. This drop of kT in the membrane at 10(4) reflected the decrease in the frequency of label collisions caused by the increase in the media viscosity and steric hindrances.
Mekler
V M
VM
Umarova
F T
FT
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D008565:Membrane Proteins / Q000032:analysis*; D010777:Photochemistry; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D013552:Swine
D008565:Membrane Proteins; D000254:Sodium-Potassium-Exchanging ATPase
Ispol'zovanie iavleniia tripletno-sensibilizirovannogo fotokhromizma dlia izucheniia dinamicheskikh vzaimodeĭstviĭ belkov v membranakh.