A change in optical rotation of creatine-ATP transphosphorylase during enzyme substrate interaction suggesting an alteration in conformation.
作者信息
SAMUELS A J, NIHEI T, NODA L
出版信息
Proc Natl Acad Sci U S A. 1961 Dec 15;47(12):1992-6. doi: 10.1073/pnas.47.12.1992.
Abstract
摘要
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A change in optical rotation of creatine-ATP transphosphorylase during enzyme substrate interaction suggesting an alteration in conformation.
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ANOMALOUS OPTICAL ROTATORY DISPERSION OF DYE: POLYPEPTIDE COMPLEXES.
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Role of the coenzyme in the stabilization of glyceraldehyde-3-phosphate dehydrogenase.
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Mechanism of enzyme action.
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Structural changes induced by the blocking of protein SH groups.
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The enzymatic activity and inhibition of adenosine 5'-triphosphate-creatine transphosphorylase.
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Optical rotation and viscosity of native and denatured proteins. XII. Differences between human and bovine albumins.
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Antibodies against enzymes.
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Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties.
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