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Digestion of Myosin by a Bacterial Protease
Authors:Jun-ichiro Morita  Tsutomu Yasui
Affiliation:Department of Animal Science, Faculty of Agriculture, Hokkaido University, Sapporo, Hokkaido
Abstract:A neutral protease, which was prepared from Bacillus polymixa, was used on the digestion of myosin. Myosin was split to HMM and LMM, The HMM fraction was further digested with the protease and a subfragment-1 was prepared.

The sedimentation coefficient,  /></span>, and the intrinsic viscosity of this subfragment-1 were determined as 5.6S and 0.08dl/g, respectively. The molecular weight was estimated to be about 120,000 by the sedimentation equilibrium method. This subfragment showed the characteristic myosin-type ATPase; the ATPase was activated by Ca<sup>2+</sup> ion or EDTA and inhibited by Mg<sup>2+</sup> ion, the maximum activation of ATPase was obtained when 3.5 SH groups per 10<sup>5</sup> g of subfragment were titrated with PCMB.</p>The subfragment-1 possessed the ability to interact with F-actin and to accelerate G-actin polymerization.</td>
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Keywords:fish collagen peptide  paracellular pathway  tight junction  permeability  Caco-2 cells
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