The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells (Q24675604)

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English	The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells	scientific article

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instance of

scholarly article

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title

The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells (English)

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author name string

V V Papov

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1

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S A Gravina

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2

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J J Mieyal

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3

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K Biemann

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4

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language of work or name

English

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publication date

March 1994

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published in

Protein Science

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volume

3

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issue

3

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page(s)

428-34

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cites work

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Reductive cleavage of cystine disulfides with tributylphosphine

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Contributions of mass spectrometry to peptide and protein structure

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Preparation of homogeneous pig liver thioltransferase by a thiol:disulfide mediated pI shift

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Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione.

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Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation

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Purification and properties of thioltransferase

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Thioltransferase from human placenta

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Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra

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High-performance tandem mass spectrometry: calibration and performance of linked scans of a four-sector instrument

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Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine

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The role of membrane protein sulfhydryl groups in hydrogen peroxide-mediated membrane damage in human erythrocytes

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A revised sequence of calf thymus glutaredoxin

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Thioltransferase in human red blood cells: purification and properties

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Thioltransferase in human red blood cells: kinetics and equilibrium

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Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase

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Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry

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The structure of partially oxygenated hemoglobin. A highly reactive intermediate toward a sulfhydryl titrant

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[10] Reductive cleavage of cystine disulfides with tributylphosphine

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Crossref

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Collision-induced fragmentation of (M + H)+ ions of peptides. Side chain specific sequence ions

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Modification of erythrocyte enzyme activities by persulfides and methanethiol: possible regulatory role

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Study on Human Erythrocyte Thioltransferase: Comparative Characterization with Bovine Enzyme and Its Physiological Role under Oxidative Stress

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Crossref

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based on heuristic

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Identifiers

DOI

10.1002/PRO.5560030307

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PMC publication ID

2142694

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PubMed publication ID

8019414

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ResearchGate publication ID

227614393

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