By Alton Meister
Advances in Enzymology and comparable parts of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative experiences of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unmatched view of the ancient improvement of enzymology. The sequence bargains researchers the newest realizing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic strategy, and their software in either the laboratory and undefined. each one quantity within the sequence positive factors contributions by way of major pioneers and investigators within the box from all over the world. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of issues and lengthy ancient pedigree, Advances in Enzymology and similar parts of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by way of any scientist drawn to the invention of an enzyme, its homes, and its functions.
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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 23
26, 608 (1957). 64. , to be published. 65. , T. Shimanouchi, and S. Mizushima, Bull. Chem. Japan, 29, 802 (1956). 66. , T. Shimanouchi, K. Kuratani, M. Tsuboi, T. Sugita, I. Nakagawa, and K. Kurosaki, Nature, 169, 1058 (1952). Advances in Enzymology and Related Areas of Molecular Biology, Volume 23 Edited by F. F. Nord Copyright © 1961 by Interscience Publishers, Inc. DENATURATION AND INACTIVATION O F ENZYME P R O T E I N S By KAZUO OKUNUKI, Osaka, Japan CONTENTS I. Introduction. . . . ..........................
The quantitative distinction between the denatured a,nd native states of a protein. This is because the methods available for detecting these changes during denaturation are too insensitive to detect slight changes in the conformation of the protein molecule. With enzyme proteins, the fourth criterion is the most useful for the determination of the “ratio of denaturation,” since many observations show that enzymic activity is lost when the enzyme protein is denatured. As described below, this is true with microbial a-amylase, catalase of bovine liver, etc.
Therefore, this method is useful only in special cases. , denatured molecules of a protein are completely digested and native ones are not digested at all-other more convenient methods, such as the Folin reaction or measurement of the ultravioletfabsorption at 278 mp, can be applied. From our results (29,35-37,71,74-77,80,81,94,95,117), it is evident, that the susceptibility of native or denatured proteins to the bacterial proteinase can be well accounted for by the “all or none” theory. Notably, in an experiment on Taka-a-amylase treated with acid, it was shown that the molecules of denatured amylase in a protein partially denatured by a mild treatment me all digested to the same extent as those completely denatured by some drastic treatment.