• Journal of Life Science
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• v.9 no.6
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• pp.646-652
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• 1999

The effect of temperature on the structure change of the SH of myosin head have been investigated with improved resolution by x-ray diffraction using synchrotron radiation. The movement of myosin head and conformational change of contractile molecules were occurred in the muscle contraction. IASL (iodo acetamide) and MSL (maleimide) disordered the orderly helix arrangement of myosin in the rest state of spin level. The temperature effect on the structure change was great at the UL in the equatorial reflection. But those of IASL and MSL were minor. Equatorial reflection (10, 11) change inferred that myosin head was moved to the vicinity of actin filament by temperature change (from $25^{\circ}C$ to $0^{\circ}C$) at UL, but spin level was not changed. The intensity change of 143 $\AA$ and 72 $\AA$ could offer information of the mass profection of population of myosin heads along the filament axis. The slope of intensity profile of the mass profection of 143$\AA$ and reflection of MSL is appeared sharply and those of UL and IASL were not changed. The decrease of MSL actin reflection at 51 $\AA$ and 59 $\AA$ in the actin reflection change refers that the shifted myosin head binds a certain actin or changes an actin structure. From these results, we could conclude that IASL and MSL were spin labeled on SH of myosin head and disordered the helix arrangement of actin.

• Journal of Life Science
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• v.8 no.6
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• pp.681-686
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• 1998

IASL(iodo acetamide) and MSL(maleimide) disordered the orderly helix arrangement of myosin in the rest state of spin level. Especially the effect of IASL was great. Equatorial reflection(10,11) change inferred that myosin head was moved to the vicinity of actin filament by spin level. The intensity change of 143 $\AA$ and 72 $\AA$ could offer infor-mation of the mass projection of population of myosin heads along the filament axis. The slope of intensity profile of the mass projection of 143 $\AA$ and reflection of IASL is appeared and that of MSL is appeared sharply. The dec-rease of 215 $\AA$ reflection intensity the periodical characteristic of 143 $\AA$ reflection by spin label. The raise of MSL actin reflection at 51 $\AA$ and 59 $\AA$ in the actin reflection change refers that the shifted myosin head binds a certain actin or changes an actin structure by spin label effect. Because iodo acetamide has a tendency to decease the actin reflection, actin dose not bind myosin head. From this result, we could conclude that LASL and MSL are spin labeled on SH of myosin head and disordered the helix arrangement of actin.

• Journal of the Korean Applied Science and Technology
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• v.22 no.1
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• pp.84-90
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• 2005

IASL(iodo acetamide) and MSL(maleimide) disordered the orderly helix arrangement of myosin in the rest state of spin level. Especially the effect of IASL was great. Equatorial refiection(10,11) change inferred that myosin head was moved to the vicinity of actin filament by spin level. The intensity change of 143${\AA}$ and 72${\AA}$ could offer information of the mass projection of population of myosin heads along the :filament axis. The slope of intensity profile of the mass projection of 143${\AA}$ and reflection of IASL is appeared and that of MSL is appeared sharply. The decrease of 215${\AA}$ reflection intensity is appeared the periodical characteristic of 143${\AA}$ reflection by spin label. The raise of MSL actin reflection at 51${\AA}$ and 59${\AA}$ in the actin reflection change refers that the shifted myosin head binds a certain actin or changes an actin structure by spin label effect. Because iodo acetamide has a tendency to decease the actin reflection, actin dose not bind myosin head. From this result, we could conclude that LASL and MSL are spin labeled on SH of myosin head and disordered the helix arrangement of actin.

• Journal of the Korean Applied Science and Technology
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• v.20 no.3
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• pp.268-273
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• 2003

IASL(iodo acetamide spin label) and MSL(maleimide spin label) disordered the orderly helix arrangement of myosin in the rest state of spin level. Especially the effect of IASL was great. The muscle was isometrically tetanized with three trains of 3ms pulses every 50ms between $5^{\circ}C$ with $25^{\circ}C$. Equatorial reflection change inferred that myosin head was moved to the vicinity of actin filament by spin level. The intensity change of $143{\AA}$ and $72{\AA}$ could offer information of the mass projection of population of myosin head along the filament axis. The slope of intensity profile of the mass projection of $143{\AA}$ and reflection of IASL is appeared and that of MSL is appeared sharply. The decrease of $215{\AA}$ reflection intensity the periodical character of $143{\AA}$ reflection by spin label. The raise of MSL actin reflection at $51{\AA}$ and $59{\AA}$ in the actin reflection change refers that the shifted myosin head binds a certain actin or changes an actin structure by spin label effect. Because iodo acetamide has a tendency to decease the actin reflection, actin dose not bind myosin head. From this result, we can conclude that IASL and MSL are spin labeled on SH of myosin head and disordered the helix arrangement of actin.

• Journal of Life Science
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• v.8 no.4
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• pp.373-380
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• 1998

A considerable change observed in X-ray diffraction during the muscle contraction was that the movement of myosin head and conformational change of contractile monecules were occurred in the muscle contraction. Time slice requires tension peak after the onset of stimulation and the height of tension peak depends on the number of twitch cycle. The intensity of I$_{11}$, I$_{10}$, 143${\AA}$ reflection is measured with 5ms time resolution and is recorded in isometric tension. The peak height of I$_{11}$ and 143${\AA}$ intensity is changed after the onset of a stimulation I$_{i}$, and the length of twitch is shortened by successive twitches in the case of stimulation TI$_{i}$. On the other hand, the peak height of I$_{11}$ and 215${\AA}$ intensity starts to decrease at the 1st twitch and remains constant at low peak hight without appreciable recovery during the contraction term. In the case of uccessive twitch stimulation, the myosin heads of muscle are once moved from their resting position and never returned to their initial position.

• Journal of the Korean Applied Science and Technology
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• v.24 no.1
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• pp.61-66
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• 2007

X-ray diffraction studies have been made to investigate the effects of binding of ADP, ADP+Vi, ADP+AIF4, $ADP+BeF_3$ on the structure of glycerinated rabbit skeletal muscle in the rigor state. Although these phosphate analogs are known to bind actively cycling myosin heads, it is not clear whether they can bind to the attached heads in the rigor muscle. We have found that these analogs can bind to the myosin heads attached to actin filaments in the rigor state. The present results indicate that (1) bound myosin heads altered their conformation in the proximal end toward the plane perpendicular to the fiber axis when MgADP bound to them, and (2) myosin heads were dissociated substantially (up to 50%) from actin filaments but still remained in the vicinity of actin filaments when MgADP and metallofluorides (AIF4 and BeF3) or vanadate bound to them. We detected new conformations of myosin heads attached to actin filaments when they had MgADP or ADP.Pi analogs. We report here these findings on the effects of MgADP and MgADP+phosphate analogs to the rigor crossbridges.

• Journal of the Korean Applied Science and Technology
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• v.24 no.4
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• pp.362-368
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• 2007

To study the relationship between elementary biochemical states and structural states of the actomyosin crossbridges in muscle, the effects of binding of MgADP to myosin heads in the rigor muscle were examined by X-ray diffraction using synchrotron radiation. X-ray diffraction studies have been made to investigate the effects of binding of ADP on the structure of glycerinated rabbit skeletal muscle in the rigor state. The intensity increase was accompanied by a slight but distinct decrease in the 5.9 am layer-line intensity close to the meridian. These results strongly suggest that myosin heads altered their attached conformation in the proximal end toward the plane perpendicular to the fiber axis when MgADP was bound to them. We found that the intensity of the 14.5 nm-based meridional reflections increase by 20-50% when MgADP was added to the rigor muscle in the presence of hexokinase and myokinase inhibitor.

• Journal of the Korean Applied Science and Technology
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• v.21 no.2
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• pp.182-189
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• 2004

On contraction of the muscles, marked changes in X-ray reflections are observed, suggesting that conformational changes of contractile molecules and the movement of myosin heads during muscle contraction. Time slice requires tension peak after the onset of stimulation and the height of tension peak depends on the number of twitch cycle. The muscles were stimulated by five successive stimuli at an interval of 80 ms started while the tension was still being exerted by the muscles. The intensity of $I_{11}$, $I_{10}$, $143{\AA}$ and $215{\AA}$ reflection measured with 5ms time resolution and is recorded in isometric tension. The peak height of $I_{11}$ and $143{\AA}$ intensity is changed after the onset of a stimulation $I_i$, and the length of twitch is shortened by successive twitches in the case of stimulation $T_i$. On the other hand, the peak height of In and $215{\AA}$ intensity starts to decrease at the 1st twitch and remains constant at low peak height without appreciable recovery during the contraction term. In the case of successive twitch stimulation, the myosin heads of muscle are once moved from their resting position and never returned to their initial position.

• The Journal of the Korea Contents Association
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• v.5 no.4
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• pp.71-77
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• 2005

On contraction of the muscles, marked changes in X-ray reflections are observed, suggesting that conformational changes of contractile molecules and the movement of myosin heads during muscle contraction. It was found that the successive twitches decreased not only the time needed to the peak tension after the onset of stimulation but also the time needed to the maximum change of the X-ray intensity. However, the difference of the time between the peak tension and the maximum intensity change$(T_i-I_i)$ is nearly the same at any twitch.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.27 no.4
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• pp.327-334
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• 1994

This study was undertaken to clarify the effect of killing methods on the morphological and histological changes of plaice, Paralichthys olivaceus muscle at early stage after killing. Killed samples by the three different methods were stored at $5^{\circ}$, and the changes in breaking strength of muscle, morphological observation of myofibrils and histological observation of extracellular spaces through storage were monitored. Samples killed by electrifying in sea water showed the maximum value of breakin strength immediately after killing and then it dropped significantly(p<0.05) until 2.5hrs passed. Breaking strength of samples killed by spiking at the head instantly and dipping in sea water including anesthetic rose steadily over 10hrs and 15hrs after killing, respectively. In myofibrills prepared from dorsal muscles immediately after spiking at the head instantly, A-band, H-band, I-band, and Z-line in sarcomere were clearly distinguishable each other. Due to muscle contraction by electrical stimulation, it was impossible to distinguish H-band from I-band observed in sarcomere immediately after killing for samples killed by electrifying. But, in the cases of samples killed by spiking and dipping, H-band could be observed dimly until 10hrs and 15hrs storage. No extracellular space was observed among muscle cells immediately after spiking at the head instantly. Samples killed by spiking at the head instantly and dipping in sea water including anesthetic showed extracellular spaces among all muscle cells after 15hrs and 25hrs storage, respectively. The other hand, samples killed by electrifying in sea water (110V, 30sec.) showed a few extracellular spaces immediately after killing and then it showed extracellular spaces among all muscle cells after 2.5hrs storage.