PMID- 3258684
OWN - NLM
STAT- MEDLINE
DCOM- 19880524
LR  - 20151119
IS  - 0041-3771 (Print)
IS  - 0041-3771 (Linking)
VI  - 30
IP  - 1
DP  - 1988 Jan
TI  - [Intravital research on hydrophobic interactions in protein fibrils using a 
      fluorescence polarization method].
PG  - 49-52
AB  - Fluorescent probe of acridine orange (AO) is known to be bound exclusively by 
      materials of thick protofibril muscle fibres. The dependence of fluorescence 
      anisotropy of AO in frog muscle fibres on the temperature has been studied. It 
      has been found that the fluorophore orientation decreases with temperature, i.e. 
      here the adsorbent cold denaturation takes place. This phenomenon was 
      demonstrated for living, skinned and glycerinated muscle fibres. It shows that 
      hydrophobic interactions contribute much to stabilization of the myosin 
      structure. After contraction of glycerinated muscle fibres at the action of ATP, 
      the AO fluorescence anisotropy grows independently of the temperature which is 
      indicative of structural rearrangements in materials of thick protofibrils upon 
      contraction.
FAU - Gamalei, I A
AU  - Gamalei IA
FAU - Kaulin, A B
AU  - Kaulin AB
LA  - rus
PT  - Comparative Study
PT  - English Abstract
PT  - Journal Article
TT  - Prizhiznennoe issledovanie gidrofobnykh vzaimodeistvii v belkovykh fibrillakh 
      poliarizatsionno-fluorestsentnym metodom.
PL  - Russia (Federation)
TA  - Tsitologiia
JT  - Tsitologiia
JID - 0417363
RN  - 0 (Muscle Proteins)
RN  - F30N4O6XVV (Acridine Orange)
RN  - PDC6A3C0OX (Glycerol)
SB  - IM
MH  - Acridine Orange
MH  - Animals
MH  - Fluorescence Polarization/methods
MH  - Glycerol/pharmacology
MH  - Muscle Proteins/*metabolism
MH  - Myofibrils/drug effects/*metabolism
MH  - Rana temporaria
MH  - Temperature
EDAT- 1988/01/01 00:00
MHDA- 1988/01/01 00:01
CRDT- 1988/01/01 00:00
PHST- 1988/01/01 00:00 [pubmed]
PHST- 1988/01/01 00:01 [medline]
PHST- 1988/01/01 00:00 [entrez]
PST - ppublish
SO  - Tsitologiia. 1988 Jan;30(1):49-52.