This article is only available in the PDF format. Download the PDF to view the article, as well as its associated figures and tables.
This monograph is edited by a distinguished group of physical chemists, kinetic energy chemists, electron microscopists, and physiologists in honor of the retiring dean and professor of Pharmacology of the University of Tokyo, Professor Hiroshi Kumagai.
The majority of contributors are well known in this country for fundamental work in muscle proteins: Ebashi for his work on α- and β-actinin and his work on native tropomyosin and troponin. The majority have worked intensively on divalent cations —in particular, the relaxing factor and its relation to Ca++ and the sarcoplasmic reticulum.
This is a scholarly physical chemistry text not written for the clinician who will find it "tough sledding." The elegant studies of adenosine triphosphate (ATP) myosin active sites by Tonomura et al demonstrating hydrogen bonding at the 6-N position of ATP adenine and of the O atom of ribose to the NHs of the peptite leakages of proline and betaine
Shy GM. Molecular Biology of Muscle Contraction.. Arch Neurol. 1966;14(5):568–569. doi:10.1001/archneur.1966.00470110112016
Customize your JAMA Network experience by selecting one or more topics from the list below.