Karaidashov, E. A., Bíró, N. A. & Panteleeva, N. S.

18 O-exchange reactions catalyzed by subfragment 1 of myosin molecule.

Biokhimiia 41, 1454-9.

18 O-exchange properties of enzymically active proteolytic fragment of myosin molecule--subfragment 1 were studied. It was shown that 18O-exchange activity of subfragment 1 is similar to that of parental myosin and its other proteolytic fragment--heavy meromyosin. The experimental data suggest that the 18O-exchange activity is an integral property of myosin and is not determined by its contaminations.

Hegyi, G; Cséke, C; Fábián, F

Iinvestigation of tryptophyl residues of actin.

Acta Biochim Biophys Acad Sci Hung 11, 221-22.

Garamvölgyi, N., Váczy, K. & Bíró, E. N.

Electron microscopic observations on the interaction of the myosin head subunit with actin in myofibrils.

Acta Biochim Biophys Acad Sci Hung 11, 279-86.

Glycerol-extracted rabbit psoas muscle fibres were treated with a solution containing the head subunits of myosin. Interaction of the isolated myosin heads with actin filaments in situ was indicated by an increase in the density of the I-band and by an increased diameter of actin filaments alongside their whole length. We conclude that actin filaments are able to interact with a considerably larger number of myosin molecules than that available in the myofibril under in vivo conditions.