A "Chest Service"

Ellman, Philip

doi:10.1016/s0140-6736(59)90346-0

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Comparison Of the Purification Of High-iron And Low-iron 5-a1

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Cited by 32 publications

(39 citation statements)

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“…min-' . mg protein-' wasmeasured with or without treatment with DTT The content of sulfhydryl groups was determined using DTNB [4].Cyanidebindingwasmeasured using ["C]cyanide. The enzyme was incubated for 15 min with 50 nmol DTNB/g protein in an anaerobic buffer containing 0.05% Triton X-100,20 mM Tris (pH 7.9 at 0°C).…”

Section: Resultsmentioning

confidence: 99%

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An essential sulfhydryl group at the substrate site of the fumarate reductase of Vibrio succinogenes

Unden

Kröger

1980

FEBS Letters

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Section: Resultsmentioning

confidence: 99%

“…This indicates that the inhibition is caused by reaction of a sulfhydryl group of the enzyme [4]. The enzyme inhibited by DTNB was reacted withlabeled cyanide and the excess of cyanide was subsequently removed by chromatography on Sephadex G-25.…”

Section: Resultsmentioning

confidence: 99%

An essential sulfhydryl group at the substrate site of the fumarate reductase of Vibrio succinogenes

Unden

Kröger

1980

FEBS Letters

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“…The free sulfhydryl content of TSP was assayed using the DTNB assay of Ellman [14] with an extinction coefficient of 1.36 x 10e4 M-'*cm-' at 412 mn for the dinitrophenol anion generated. The intactness of TSP before and after spin labeling was examined by SDS-PAGE as described by Laemmli [15].…”

Section: Other Methodsmentioning

confidence: 99%

Conformational change in thrombospondin induced by removal of bound Ca²⁺ A spin label approach

1988

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The effect of removal of Ca*+ bound to thrombospondin (TSP) on the protein structure in solution has been investigated using ESR spin-label techniques. A maleimide spin label was selectively attached to the free thiol group presumably near the carboxyl-terminal domain in which Ca 2+-binding sites are situated. The ESR spectra of spin-labeled TSP showed that the bound label undergoes a relatively fast rotational motion with an effective rotational correlation time in the nanosecond time regimes. Removal of bound C3+ in TSP by dialyzing spin-labeled TSP from a Ca*+-containing buffer into an EDTA-containing buffer resulted in an increase in the mobility of the bound label by a factor of 2.3. The data suggest that EDTA chelation of bound Caz+ in TSP induces a conformational change of TSP at least near the site of spin labeling.

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“…-SH groups are titrated by DTNB [9] in 6 M urea, pH 8.2. Amino acid analysis were carried out on a TSM 1 Technicon autoanalyser.…”

Section: Methodsmentioning

confidence: 99%

Essential carboxyl groups in yeast hexokinase

Pho¹,

Roustan²,

Desvages³

et al. 1974

FEBS Letters

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A "Chest Service"

Cited by 32 publications

References 6 publications

An essential sulfhydryl group at the substrate site of the fumarate reductase of Vibrio succinogenes

An essential sulfhydryl group at the substrate site of the fumarate reductase of Vibrio succinogenes

Conformational change in thrombospondin induced by removal of bound Ca²⁺ A spin label approach

Essential carboxyl groups in yeast hexokinase

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A "Chest Service"

Cited by 32 publications

References 6 publications

An essential sulfhydryl group at the substrate site of the fumarate reductase of Vibrio succinogenes

An essential sulfhydryl group at the substrate site of the fumarate reductase of Vibrio succinogenes

Conformational change in thrombospondin induced by removal of bound Ca2+ A spin label approach

Essential carboxyl groups in yeast hexokinase

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Conformational change in thrombospondin induced by removal of bound Ca²⁺ A spin label approach