Studies of the Enzyme Fumarase. II.1 Isolation and Physical Properties of Crystalline Enzyme

Car Frieden; Robert M. Bock; Robert A. Alberty

doi:10.1021/ja01638a052

Studies of the Enzyme Fumarase. II.¹ Isolation and Physical Properties of Crystalline Enzyme

Car Frieden, Robert M. Bock, Robert A. Alberty

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Abstract

A method is described for the isolation and crystallization of fumarase from pig heart muscle which differs from methods which have previously been reported. Based on the muscle extract, a 2600-fold increase in specific activity and a recovery of 20% are obtained. This protein yields a single boundary in the electrophoresis apparatus and in the velocity ultracentrifuge. The ultraviolet absorption is characteristic of a protein, and it has not been possible to detect an enzyme-substrate complex spectrophotometrically.

Original language	English
Pages (from-to)	2482-2484
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	76
Issue number	9
DOIs	https://doi.org/10.1021/ja01638a052
State	Published - May 1954

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abstract = "A method is described for the isolation and crystallization of fumarase from pig heart muscle which differs from methods which have previously been reported. Based on the muscle extract, a 2600-fold increase in specific activity and a recovery of 20% are obtained. This protein yields a single boundary in the electrophoresis apparatus and in the velocity ultracentrifuge. The ultraviolet absorption is characteristic of a protein, and it has not been possible to detect an enzyme-substrate complex spectrophotometrically.",

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year = "1954",

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AU - Alberty, Robert A.

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N2 - A method is described for the isolation and crystallization of fumarase from pig heart muscle which differs from methods which have previously been reported. Based on the muscle extract, a 2600-fold increase in specific activity and a recovery of 20% are obtained. This protein yields a single boundary in the electrophoresis apparatus and in the velocity ultracentrifuge. The ultraviolet absorption is characteristic of a protein, and it has not been possible to detect an enzyme-substrate complex spectrophotometrically.

AB - A method is described for the isolation and crystallization of fumarase from pig heart muscle which differs from methods which have previously been reported. Based on the muscle extract, a 2600-fold increase in specific activity and a recovery of 20% are obtained. This protein yields a single boundary in the electrophoresis apparatus and in the velocity ultracentrifuge. The ultraviolet absorption is characteristic of a protein, and it has not been possible to detect an enzyme-substrate complex spectrophotometrically.

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Studies of the Enzyme Fumarase. II.¹ Isolation and Physical Properties of Crystalline Enzyme

Abstract

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