ABSTRACT
Method of scanning calorimetry of intact and denervated F-actin shows a change in thermostability of protein after denervation.
Subject(s)
Actins/analysis , Muscle Denervation , Muscles/analysis , Animals , Calorimetry, Differential Scanning , RabbitsABSTRACT
Method of circular dichroism did not indicate any changes of the secondary structure of globular and fibrillar actin from denervated skeletal muscles. The matter that some conformational changes of the aromatic residues do in fact accompany denervation was confirmed by fluorescence studies but not by CD spectra.
Subject(s)
Actins/analysis , Muscle Denervation , Muscles/analysis , Animals , Circular Dichroism , RabbitsABSTRACT
Spectra of tryptophan UV-fluorescence and UV-absorption of myosin isolated 30 days after denervation of white skeletal muscles of rabbit were studied. It has been observed that fluorescence intensity of such myosin in the maximum decreases. This decrease becomes more pronounced after purification of protein from admixtures. It has been shown that after denervation the absorption at 260 nm increases, however, the difference disappears after myosin purification. The data obtained point to a change of myosin structural state after denervation.
Subject(s)
Muscles/analysis , Myosins/analysis , Animals , Muscle Denervation , Rabbits , Spectrophotometry, UltravioletABSTRACT
The cation dye acridine orange (AO) was shown to inhibit ATPase activity of myosin, DTNB-myosin and heavy meromyosin and not to influence that of EDTA-S-1 at low ionic force. The inhibiting effect is concerned with the presence of KCl in solution. The allosteric influence of AO on myosin ATPase activity is discussed and dependence of this effect on charge distribution on the surface of the protein molecule is considered.
Subject(s)
Acridine Orange/pharmacology , Adenosine Triphosphatases/antagonists & inhibitors , Myosins/antagonists & inhibitors , Animals , Dithionitrobenzoic Acid/pharmacology , Kinetics , Myosin Subfragments/metabolism , RabbitsABSTRACT
Amino acid composition of actin from white skeletal muscles of the rabbit was studied 14 and 50 days after denervation. The content of valine, histidine and tyrosine was shown to decrease and that of lysine and leucine to increase on the 14th day following denervation. The content of these amino acids was almost normalised on the 50th day. In case of actin obtained from the contralateral leg similar but less pronounced changes were revealed. The results obtained are discussed as to the role played by some of amino acids in actin polymerization.
Subject(s)
Actins/metabolism , Muscle Denervation , Muscles/metabolism , Amino Acids/analysis , Animals , Kinetics , RabbitsABSTRACT
Superprecipitation of synthetic actomyosin formed from intact myosin and actin extracted from rabbit white skeletal muscles after denervation was compared with that of intact synthetic actomyosin. Superprecipitation was characterized by two parameters: (1) the value of superprecipitation delta E determining an increase in the absorption from minimum to maximum values, and (2) the time required for the half-maximum increase (t1/2) which is inverse of the velocity constant. It was shown that delta E and the velocity constant decrease and t1/2 after denervation. It is assumed that this effect is related to the changes in actin structure.
Subject(s)
Actins/metabolism , Actomyosin/metabolism , Muscle Denervation , Muscles/metabolism , Animals , Chemical Precipitation , Kinetics , Myosins/metabolism , RabbitsSubject(s)
Muscle Denervation , Muscle Proteins/analysis , Myofibrils/analysis , Animals , Electrophoresis, Disc , Rabbits , Sodium Dodecyl Sulfate , UreaABSTRACT
Effect of superviscous state of AO stained actin in concentrated salts (KCI) significantly decreases two weeks after denervation. These changes of anomalous behaviour of stained action are partially reversible at the long time diasrophy. This phenomenon is suggested to be connected with the structural changes of "denervated" actin, which are reflected in the changes of protein electrostatic region.
