Isolation of Carp Myosin Rod and Its Structural Stability.

Abstract

Carp myosin rod was isolated from the chymotryptic digest of myosin by using DEAE-Toyo pearl chromatography.The carp rod thus prepared was very similar to rabbit rod in its molecular mass, viscosity, sedimentation velocity, and amino acid composition . Changes in tryptophan fluorescence intensity indicated that carp rod more easily unfolded upon addition of urea or gua nidine-HCI, and thus was structurally less stable than rabbit rod . It was found that the addition of 8-anilino-1-naphthalene sulfonate (ANS) to carp rod solution resulted in no change in fluore rescence intensity, providing no information on its structural stability . However, ANS was an excellent probe for detecting the structural change of myosin subfragment-1 (S-1) portion; namely carp S-1 required a lower urea concentration than rabbit S-1 for inducing an increase inthe ANS fluorescence intensity.

Recovery of Tilapia (Oreochromis niloticus) Protein Isolate by High-Intensity Ultrasound-Aided Alkaline Isoelectric Solubilization/Precipitation Process

“…This agreed with the results of Kristinsson and Hultin (2003b) that alkaline treatment caused the misfolding of the myosin head fraction and led to increased surface hydrophobicity, the reason of which was ascribed to more hydrophobic clusters becoming exposed at alkaline pH. Kato and Konno (1993) found that the myosin head was responsible for almost all of the ANS-binding capacity. It was noted that two HIUs enhanced the surface hydrophobicity of the proteins (treatments 4, 8, and 12) compared to that of the corresponding control (treatments 1, 5, and 9) as well.…”

Responsibility of Myosin Rod for the Dimer Formation of Myosin Heavy Chain through SS Bonding during Ice Storage of Carp Actomyosin

“…The resulting solution was centrifuged at Abbreiviation: EDTA, Ethylenediaminetetraacetic acid; MHC, Myosin heavy chain; MSH, 2-Mercaptoethanol; PMSF, Phenylmethylsulfonylfluo ride; SDS-PAGE , Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis; SHa, one sulfhydryl group on myosin tail region responsible for the activation of Mg2+-ATPase; SH1 , one reactive sulfhydryl group on myosin head region related to Ca2+-ATPase activity; S-1, Myosin subfragment-1. rod, the size of which is in excellent agreement with the size of S-1 and rod reported by Kato and Konno.7,8) Changes in SH content are shown in Fig. 2.…”

Effect of calcium ion on the thermal denaturation of subfragment-1 and rod regions of squid myosin upon the heating of myofibrils

“…Rod in the digest was purified by using ammonium sulfate fractionation as previously described [15]. Myosin rod was finally dissolved in 0.5 M KCl, 20 mM Tris-HCl (pH 7.5).…”