Role of the intersubunit disulfide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphatase
- 15 August 1996
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1296 (1) , 76-84
- https://doi.org/10.1016/0167-4838(96)00055-6
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Structural relationship between the mammalian Fe(III)‐Fe(II) and the Fe(III)‐Zn(II) plant purple acid phosphatasesFEBS Letters, 1995
- Crystal Structure of a Purple Acid Phosphatase Containing a Dinuclear Fe(III)-Zn(II) Active SiteScience, 1995
- Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturationProtein Science, 1994
- The Amino Acid Sequence of the Red Kidney Bean Fe(III)‐Zn(II) Purple Acid PhosphataseEuropean Journal of Biochemistry, 1994
- Comparative Equilibrium Denaturation Studies of the Neurotrophins: Nerve Growth Factor, Brain-Derived Neurotrophic Factor, Neurotrophin 3, and Neurotrophin 4/5Biochemistry, 1994
- Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediateBiochemistry, 1990
- Equilibrium dissociation and unfolding of the arc repressor dimerBiochemistry, 1989
- Properties of a purple phosphatase from red kidney bean: a zinc-iron metalloenzymeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Evidence for an intermediate in the denaturation and assembly of phosphoglucose isomeraseArchives of Biochemistry and Biophysics, 1981
- Protein DenaturationAdvances in Protein Chemistry, 1968