Malate dehydrogenase. XI. Absence of tryptophan in porcine heart mitochondrial enzyme

N. L. Eberhardt; R. G. Wolfe

doi:10.1016/S0003-9861(74)80020-2

Malate dehydrogenase. XI. Absence of tryptophan in porcine heart mitochondrial enzyme

N. L. Eberhardt, R. G. Wolfe

Endocrinology, Diabetes, Metabolism, and Nutrition

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Native and guanidine hydrochloride-denatured pig heart mitochondrial malate dehydrogenase have fluorescence and phosphorescence emission spectra resembling tyrosine but not that of tryptophan. Furthermore, amino acid analysis of acid and alkaline hydrolysates of the pure enzyme, designed to detect 0.15 tryptophan residues or more per subunit, failed to show detectable quantities. It is confirmed that the enzyme lacks tryptophan and this amino acid can have no function in the catalytic mechanism.

Original language	English (US)
Pages (from-to)	151-155
Number of pages	5
Journal	Archives of Biochemistry and Biophysics
Volume	160
Issue number	1
DOIs	https://doi.org/10.1016/S0003-9861(74)80020-2
State	Published - Jan 1974

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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title = "Malate dehydrogenase. XI. Absence of tryptophan in porcine heart mitochondrial enzyme",

abstract = "Native and guanidine hydrochloride-denatured pig heart mitochondrial malate dehydrogenase have fluorescence and phosphorescence emission spectra resembling tyrosine but not that of tryptophan. Furthermore, amino acid analysis of acid and alkaline hydrolysates of the pure enzyme, designed to detect 0.15 tryptophan residues or more per subunit, failed to show detectable quantities. It is confirmed that the enzyme lacks tryptophan and this amino acid can have no function in the catalytic mechanism.",

author = "Eberhardt, {N. L.} and Wolfe, {R. G.}",

note = "Funding Information: Unless otherwise stated, all reagents were Mallinckrodt analytical grade. Thiodiglycol and i This research was supported by Grant No. 5 I~OI HE-0 3226 from the National Heart Institute, U.S. Public Health Service. Funding Information: Predoctoral Trainee supported by Public Health Service Training Grant 2T01 GM00444. This paper includes research submitted by N. L. Eberhardt in partial fulfillment of requirements for the Ph.D. degree, University of Oregon, 1972.",

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N2 - Native and guanidine hydrochloride-denatured pig heart mitochondrial malate dehydrogenase have fluorescence and phosphorescence emission spectra resembling tyrosine but not that of tryptophan. Furthermore, amino acid analysis of acid and alkaline hydrolysates of the pure enzyme, designed to detect 0.15 tryptophan residues or more per subunit, failed to show detectable quantities. It is confirmed that the enzyme lacks tryptophan and this amino acid can have no function in the catalytic mechanism.

AB - Native and guanidine hydrochloride-denatured pig heart mitochondrial malate dehydrogenase have fluorescence and phosphorescence emission spectra resembling tyrosine but not that of tryptophan. Furthermore, amino acid analysis of acid and alkaline hydrolysates of the pure enzyme, designed to detect 0.15 tryptophan residues or more per subunit, failed to show detectable quantities. It is confirmed that the enzyme lacks tryptophan and this amino acid can have no function in the catalytic mechanism.

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Malate dehydrogenase. XI. Absence of tryptophan in porcine heart mitochondrial enzyme

Abstract

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