Iodination of glyceraldehyde 3-phosphate dehydrogenase

scientific article published on September 1, 1970

Iodination of glyceraldehyde 3-phosphate dehydrogenase is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1042/BJ1190307
P953full work available at URLhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/5530750/?tool=EBI
https://europepmc.org/articles/PMC1179354
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/5530750/pdf/?tool=EBI
https://europepmc.org/articles/PMC1179354?pdf=render
https://portlandpress.com/biochemj/article-pdf/119/2/307/768799/bj1190307.pdf
P932PMC publication ID1179354
P698PubMed publication ID5530750
P5875ResearchGate publication ID17652658

P2093author name stringJ. O. Thomas
J. I. Harris
P2860cites workSelective Reaction of Tyrosyl Side Chains with Iodine in d-Glyceraldehyde 3-Phosphate Dehydrogenase. 1. Study of the Differential Formation of Monoiodo and Diiodo DerivativesQ71562278
Selective Reaction of Tyrosyl Side Chains with Iodine in d-Glyceraldehyde 3-Phosphate Dehydrogenase. 2. Isolation of the Peptides Containing Reactive Tyrosyl Side ChainsQ71562280
The properties of thyroglobulin. XV. The function of the protein in the control of diiodotyrosine synthesisQ72223015
The Mechanism of Inactivation of Glyceraldehyde 3-Phosphate Dehydrogenase by Tetrathionate, o-Iodosobenzoate, and Iodine MonochlorideQ72359649
The reactivity of the sulfhydryl groups of lobster muscle glyceraldehyde 3-phosphate dehydrogenaseQ72378936
Subunit structure of hog thyroglobulin: dissociation of noniodinated and highly iodinated preparationsQ72406587
Crystallisation and comparative studies of D-3-phosphoglyceraldehyde dehydrogenase from muscle of various mammalsQ74128284
THE COMPARATIVE ENZYMOLOGY OF TRIOSEPHOSPHATE DEHYDROGENASEQ76959925
EFFECT OF TETRATHIONATE ON THE STABILITY AND IMMUNOLOGICAL PROPERTIES OF MUSCLE TRIOSEPHOSPHATE DEHYDROGENASESQ77094304
Separation of the iodized compounds of serum and the thyroid by filtration on dextran gel (Sephadex)Q78986937
Halogenation of tyrosine during acid hydrolysisQ79613483
The disulphide bonds of insulinQ24534104
The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzymeQ36385383
The use of maleic anhydride for the reversible blocking of amino groups in polypeptide chainsQ42938457
The amino acid sequence around the reactive serine residue of some proteolytic enzymesQ42962976
Structure of Glyceraldehyde-3-Phosphate Dehydrogenase: Structural Symmetry Within the MoleculeQ58963457
Role of the Coenzyme in the Stabilization of Glyceraldehyde-3-phosphate DehydrogenaseQ59051885
Glyceraldehyde 3-Phosphate Dehydrogenase from Pig MuscleQ59056349
Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide GroupsQ59061104
Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster MuscleQ59076368
Effect of Urea on Trypsin and Alpha-ChymotrypsinQ59086065
Chemical Nature of the Catalytic Sites in Glyceraldehyde-3-Phosphate DehydrogenaseQ59086791
Coenzyme-induced changes in the optical rotatory dispersion properties of glyceraldehyde 3-phosphate dehydrogenaseQ68553044
Studies of conformational changes in glyceraldehyde-3-phosphate dehydrogenase accompanying its catalytic actionQ68555364
An artefact caused by the binding of protein to dextran gelQ70095168
The reaction of sulfhydryl groups of dehydrogenases with iodineQ71225816
P433issue2
P407language of work or nameEnglishQ1860
P1104number of pages10
P304page(s)307-316
P577publication date1970-09-01
P1433published inBiochemical JournalQ864221
P1476titleIodination of glyceraldehyde 3-phosphate dehydrogenase
P478volume119

Reverse relations

cites work (P2860)
Q391730646 The use of logarithmic plots of electrophoretic mobilities of peptides
Q77919701Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme from baker's yeast
Q93746304Identification of the iodine-sensitive tyrosines in porcine pepsin
Q40005660Iodination of glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus
Q70455881Iodination of horse liver alcohol dehydrogenase

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