Studies on the subunit structure of thermostable glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference38 articles.
1. The Amino Acid Composition and Other Properties of Thermostable Glyceraldehyde 3-Phosphate Dehydrogenase from Bacillus stearothermophilus
2. Subunit structure of glyceraldehyde-3-phosphate dehydrogenase
3. Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster Muscle
4. Glyceraldehyde 3-Phosphate Dehydrogenase from Pig Muscle
5. Some observations of the sedimentation of chicken heart glyceraldehyde 3-phosphate dehydrogenase
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1. Structural basis for the thermal stability of glyceraldehyde-3-phosphate dehydrogenases;International Journal of Peptide and Protein Research;2009-01-12
2. Bacillus stearothermophilusGlyceraldehyde-3-phosphate Dehydrogenase as a Source of Angiotensin-converting Enzyme Inhibitors;Agricultural and Biological Chemistry;1990-08
3. Conformational studies on the inactivation of glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans KU;Archives of Biochemistry and Biophysics;1984-08
4. Structure-stability relationships in proteins: new approaches to stabilizing enzymes;Enzyme and Microbial Technology;1984-02
5. D-Glyceraldehyde-3-Phosphate Dehydrogenase. The Purification and Characterisation of the Enzyme from the Thermophiles Bacillus stearothermophilus and Thermus aquaticus;European Journal of Biochemistry;1980-07
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