[Study of properties of the actomyosin complex using photo-cleavage of proteins by vanadates].
Study of myosin and actomyosin preparations photocleavage conditioned by polyvanadates confirmed the data on V1 and V2 centre cleavage independence of bivalent cations. Actin does not change sufficiently the reaction in V1 centre and considerably slows down the reaction in V2 centre. These actin properties do not depend on bivalent cation (Mg2+), nor on preliminary incubation with vanadate. It was also discovered that preincubation with vanadate in EDTA medium results in myosin molecule cleavage with producing light (M 18 kD) fragments in both cases: with myosin and actomyosin preparations. Besides vanadate-dependent photocleavage of myosin peptide bonds, there were discovered photocrosslinkings of polypeptide chains in myosin and actomyosin preparations also depending on the presence of vanadate. In actomyosin preparations they probably lead to crosslinking of heavy minor proteins to heavy myosin chains.
Bukatina
A E
AE
Alievskaia
L L
LL
Neshkova
M N
MN
Torbina
N N
NN
D000205:Actomyosin / Q000737:chemistry*; D002413:Cations, Divalent; D004591:Electrophoresis, Polyacrylamide Gel; D008274:Magnesium / Q000737:chemistry; D009218:Myosins / Q000737:chemistry; D010777:Photochemistry; D014638:Vanadates / Q000737:chemistry*
D002413:Cations, Divalent; D014638:Vanadates; D000205:Actomyosin; D009218:Myosins; D008274:Magnesium
Issledovanie svoĭstv aktomiozinovogo kompleksa s pomoshch'iu obuslovlennogo vanadatami fotorasshchepleniia belkov.