Enzyme and Enzyme Fragments Purifiation by Specific Immunoadsorbents. Application to Structural Studies of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1974.tb03352.x/fullpdf
Reference9 articles.
1. Subunits of the complex protein carrying the threonine-sensitive aspartokinase activity in a mutant of Escherichia coli K 12
2. Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits
3. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12. The Two Catalytic Activities Are Carried by Two Independent Regions of the Polypeptide Chain
4. Isoleucine and Valine Metabolism of Escherichia coli XV. Biochemical Properties of Mutants Resistant to Thiaisoleucine
5. 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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1. Use of dye pseudo-affinity chromatography in the purification of homoserine dehydrogenase;Journal of Chromatography A;1991-01
2. Purification of human spleen ribonuclease by immunoabsorption. Similarity of the enzyme with human liver ribonuclease.;Journal of Biological Chemistry;1976-09
3. Multifunctional Proteins;Annual Review of Biochemistry;1976-06
4. Cyanobacterial DNA-binding protein related to Escherichia coli HU.;Proceedings of the National Academy of Sciences;1976-06-01
5. Purification by Immunoadsorbtion Chromatography of the Normal and a Mutant Form of the B2 Subunit of Escherichia coli Tryptophan Synthase;European Journal of Biochemistry;1976-04
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