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Ammonium sulfate fractionation and divalent cation precipitation were applied to purify major contractile proteins from relaxed actomyosin extracted from molluscan catch muscle myofibrils, as a supramolecular complex composed of twitchin (TW), myosin (MY), and myorod (MR). The phosphorylation of twitchin by PKA-like kinase and the phosphorylation of myosin and myorod by myosin-associated kinase were found to play crucial role in the development of the catch state.

The intrinsic, as well as the extrinsic pathways are studied to explain the relation existing between apoptosis and histone H1 phosphorylation in Jurkat cells after the induction of apoptosis. The H1 subtypes are shown to get dephosphorylated on the addition of apoptosis.

Histone acetyltransferases CREB-binding protein (CBP), p300/CBP-associated factor (PCAF), and Tat-interactive protein, 60 kDa (Tip60) is experimented for their ability to in vitro acetylate high-mobility group box-containing proteins 1 and 2(HMGB-1 and -2) and the role of C-terminal domain on the pattern of acetylation as well as some properties of the modified truncated protein. It is found that the modifications in the acetylation pattern of HMGB-1 and -2 upon removal of the C-terminal tail are regarded as a means by which the acidic domain modulates some properties of these proteins.