Mühlrad, A., Corsi, A. & Granata, A. L.

Studies on the properties of chemically modified actin. I. Photooxidation, succinylation, nitration.

Biochim Biophys Acta 162, 435-43.

Mühlrad, A.

Studies on the properties of chemically modified actin. II. Trinitrophenylation.

Biochim Biophys Acta 162, 444-51.

Hegyi, G., Mühlrad, A.

Effect of diethylpyrocarbonate on proteins. II. On the role of histidyl residues in heavy meromyosin ATPase.

Acta Biochim. Biophys. Acad. Sci. Hung 30, 425-430.

Gráf, L., Bíró, N. A. & Kovács, P.

Studies on protein complexes of muscle by means of proteolysis. IV. Further data on the tryptic digestion of myosin in the presence of Ca2+ ions.

Acta Biochim Biophys Acad Sci Hung 3, 239-46.

Fábián, F. & Mühlrad, A.

Effect of trinitrophenylation on myosin ATPase.

Biochim Biophys Acta 162, 596-603.

Abstract 1. The enzymic and actin binding properties of myosins trinitrophenylated to different extents in the presence or absence of ATP have been studied. 2. The enzymic properties of myosin trinitrophenylated in the absence of ATP are different from those of myosin treated in the presence of ATP even on trinitrophenylating an equal number of lysyl residues. On trinitrophenylation in the absence of ATP the EDTA-(K+-)activated ATPase and Ca2+-activated ATPase decrease while the Mg2+-activated ATPase considerably increases. In the presence of ATP the enzymic properties of myosin are much less affected by trinitrophenylation. 3. The actin binding capacity of trinitrophenylated myosin does not change, although its enzymic properties may be greatly altered, and even if its property to be activated by actin is completely lost.

Bálint, M., Szilágyi, L., Fekete, G., Blazso, M. & Bíró, N. A.

Studies on proteins and protein complexes of muscle by means of proteolysis. V. Fragmentation of light meromyosin by trypsin.

J Mol Biol 37, 317-30.