The Acetate Activating Enzyme System of Heart Muscle

Beinert, Helmut; Green, D.E.; Hele, Priscilla; Hift, Helen; Korff, R.W. Von; Ramakrishnan, C. V.

doi:10.1016/s0021-9258(19)52611-4

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Gus a Ropp Oak Ridge1

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1954

2022

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Cited by 217 publications

(3 citation statements)

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“…Assay of B activity was carried out by measuring both its ability to catalyze the conversion of indole into tryptophan in the presence of A protein, and its ability to stimulate the conversion of indoleglycerol phosphate into indole by the A protein (Smith and Yanofsky, 1962). Salt-free hydroxylamine was prepared according to Beinert et al (1953).…”

Section: Methodsmentioning

confidence: 99%

Subunit structure of the B component of Escherichia coli tryptophan synthetase

Hathaway¹,

Kida²,

Crawford³

1969

Biochemistry

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Section: Methodsmentioning

confidence: 99%

Subunit structure of the B component of Escherichia coli tryptophan synthetase

Hathaway¹,

Kida²,

Crawford³

1969

Biochemistry

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“…Vernon F. Raaen Received March 1, 1954 (6) This paper is based upon work performed under Contract Number W-7405-eng-26 for the Atomic Energy Commission at Oak Ridge National Laboratory.…”

Section: Gus a Ropp Oak Ridgementioning

confidence: 99%

Chromatography of Proteins on Cellulose Ion-Exchangers

Sober¹,

Peterson²

1954

J. Am. Chem. Soc.

185

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“…There was no inhibition of conversion of mevalonate-5-pyrophosphate to isopentenylpyrophosphate in the presence of avidin (Table III). Cu-Mevalonate-5-pyrophosphate (8000 cpm) was incubated with decarboxylase in the presence of salt-free hydroxylamine (either 0.4 µ or 0.8 m final concentration) (Beinert et al, 1953). There was less than 5% inhibition of the conversion of mevalonate-5-pyrophosphate to isopentenylpyrophosphate (Table III) and no detectable formation of hydroxamate.…”

mentioning

confidence: 99%