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Edited by S. Ebashi; F. Oosawa; T. Sekine; and Y. Tonomura. Price, not given. Pp 206. Elsevier Press Inc., 110 Spaistrast, Amsterdam C., Netherlands.

G. Milton Shy, MD, Reviewer

Arch Neurol. 1966;14(5):568-569.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

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 - 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 . . . [Full Text PDF of this Article]

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