경직상태의 근육막에 MgADP를 첨가시킨 결과에 대한 연구
(주)코리아스칼라
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- 2016.04.02
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- 2007.12
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서지정보
ㆍ발행기관 : 한국유화학회
ㆍ수록지정보 : 韓國油化學會誌 / 24권 / 4호
ㆍ저자명 : 김덕술
영어 초록
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.
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