(Q28208133)

1

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S Ma

2

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R M Caprioli

3

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K E Hill

4

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R F Burk

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

11 May 2001

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published in

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volume

276

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page(s)

15823-31

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issue

19

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cites work

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Centrilobular endothelial cell injury by diquat in the selenium-deficient rat liver

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Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein p

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The properties of a rat serum protein labelled by the injection of sodium selenite

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Isoforms of selenoprotein P in rat plasma. Evidence for a full-length form and another form that terminates at the second UGA in the open reading frame

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The measurement of amino groups in proteins and peptides

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Ethoxyformylation of proteins. Reaction of ethoxyformic anhydride with .alpha.-chymotrypsin, pepsin, and pancreatic ribonuclease at pH 4

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41 Modification of histidyl residues in proteins by diethylpyrocarbonate

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Evidence of an essential histidine residue in thermolysin.

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Substrate-decreased modification by diethyl pyrocarbonate of two histidines in isocitrate lyase from Escherichia coli

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Site-directed mutagenesis and chemical modification of histidine residues on an alpha-class chick liver glutathione S-transferase CL 3-3. Histidines are not needed for the activity of the enzyme and diethylpyrocarbonate modifies both histidine and l

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Selective biochemical modification of functional residues in recombinant human macrophage colony-stimulating factor beta (rhM-CSF beta): identification by mass spectrometry

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Determination of diethylpyrocarbonate-modified amino acid residues in alpha 1-acid glycoprotein by high-performance liquid chromatography electrospray ionization-mass spectrometry and matrix-assisted laser desorption/ionization time-of-flight-mass s

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Pigment epithelium-derived factor (PEDF) binds to glycosaminoglycans: analysis of the binding site.

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Chemical modification of 3 alpha,20 beta-hydroxysteroid dehydrogenase with diethyl pyrocarbonate. Evidence for an essential, highly reactive, lysyl residue

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Binding of selenoprotein P to heparin: characterization with surface plasmon resonance

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Heparinase I from Flavobacterium heparinum. Mapping and characterization of the heparin binding domain

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Further characterization of the interaction of histidine-rich glycoprotein with heparin: evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in hepar

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Importance of specific amino acids in protein binding sites for heparin and heparan sulfate

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Heparin-affinity patterns and composition of extracellular superoxide dismutase in human plasma and tissues

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Human copper-containing superoxide dismutase of high molecular weight

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The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis.

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Multiple forms of selenoprotein P in rat plasma

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Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal

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Structure characterization of functional histidine residues and carbethoxylated derivatives in peptides and proteins by mass spectrometry

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Chemical modification monitored by electrospray mass spectrometry: a rapid and simple method for identifying and studying functional residues in enzymes

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Mapping the heparin-binding site of mucus proteinase inhibitor

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Effects of acidosis on the post-hypoxic recovery of synaptic transmission in gerbil hippocampal slices

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