- 영문명
- A Study on the Middle Step of Rabbit Skeletal Muscle Membrane Contraction by Analog Effects
- 발행기관
- 한국응용과학기술학회 (구.한국유화학회)
- 저자명
- 김덕술(Kim DuckSool)
- 간행물 정보
- 『한국응용과학기술학회지』한국유화학회지 제24권 제1호, 61~66쪽, 전체 6쪽
- 주제분류
- 공학 > 화학공학
- 파일형태
- 발행일자
- 2007.03.31

국문 초록
영문 초록
X-ray diffraction studies have been made to investigate the effects of binding of ADP, ADP+Vi, ADP+AIF4, ADP+BeF3 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.
목차
해당간행물 수록 논문
참고문헌
최근 이용한 논문
교보eBook 첫 방문을 환영 합니다!
신규가입 혜택 지급이 완료 되었습니다.
바로 사용 가능한 교보e캐시 1,000원 (유효기간 7일)
지금 바로 교보eBook의 다양한 콘텐츠를 이용해 보세요!
