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Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits (Q54644560)

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scientific article published on August 4, 1972

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English	Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits	scientific article published on August 4, 1972

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scholarly article

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Europe PubMed Central

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2 June 2018

http://europepmc.org/abstract/MED/4562989

Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits (English)

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10.1111/J.1432-1033.1972.TB01938.X

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Escherichia coli

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10.1111/J.1432-1033.1972.TB01938.X

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J Janin

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F. Falcoz-Kelly

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J. C. Saari

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M. Véron

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1 August 1972

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4 August 1972

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10.1111/J.1432-1033.1972.TB01938.X

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http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1972.tb01938.x/fullpdf

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10.1111/J.1432-1033.1972.TB01938.X

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Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels

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The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of the protein catalyzing the two activities

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The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. Subunit Structure of the Protein Catalyzing the Two Activities

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Active subunits of the aspartokinase-homoserine dehydrogenase I complex from Escherichia coli

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Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 . Subunit molecular weight and nicotinamide-adenine dinucleotide phosphate binding

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The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Binding of threonine and of pyridine nucleotides: stoichiometry and optical effects

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Threonine-sensitive aspartokinase-homoserine dehydrogenase of Escherichia coli K 12. Reaction with 6-mercapto-9- -D-ribofuranosylpurine 5'-triphosphate

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Use of Dimethyl Suberimidate, a Cross-Linking Reagent, in Studying the Subunit Structure of Oligomeric Proteins

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Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH gradients. IV. Further studies on the resolving power in connection with separation of myoglobins

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Sulfenyl Halides as Modifying Reagents for Polypeptides and Proteins. Quantitative Evaluation of Tryptophan and Cysteine Residues in Proteins

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Combinations of specific color reactions useful in the peptide mapping technique

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Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*

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THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551

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Separation of dansyl-amino acids by polyamide layer chromatography

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Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups

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A Protein Sequenator

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Circular dichroic and optical rotatory dispersion spectra of the threonine-inhibited aspartokinase-homoserine dehydrogenase of Escherichia coli K 12. Effects of ligand binding and protein denaturation

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PARALLEL MODIFICATIONS CAUSED BY MUTATIONS IN TWO ENZYMES CONCERNED WITH THE BIOSYNTHESIS OF THREONINE IN ESCHERICHIA COLI

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Determination of molecular weight of proteins and protein subunits in the presence of 6M guanidine hydrochloride

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Rétro-inhibition et répression de l'homosérine déshydrogénase d'Escherichia coli

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The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. A Study of the Allosteric Equilibrium

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The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Relaxations of the allosteric equilibrium

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

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Enzyme Evolution: Generation of a Bifunctional Enzyme by Fusion of Adjacent Genes

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Tertiary structure of Escherichia coli β-d-galactosidase

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10.1111/J.1432-1033.1972.TB01938.X

1 reference

Europe PubMed Central

PubMed publication ID

2 June 2018

http://europepmc.org/abstract/MED/4562989

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 June 2018

http://europepmc.org/abstract/MED/4562989

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