Nuclear-Magnetic-Resonance Studies of Carboxypeptidase B. Binding of Inhibitors to the Manganese Enzyme
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1975.tb04018.x/fullpdf
Reference22 articles.
1. The Role of a Tyrosyl Residue in the Mechanism of Action of Carboxypeptidase B: Luminescence Studies
2. 2. J. E. Folk, and P. D. Boyer (1971 ) inThe Enzyme () 3rd ed. , vol. 3 , pp.57 -77 , Academic Press, New York.
3. Metallocarboxypeptidases: A cadmium — Carboxypeptidase B with peptidase activity
4. Basic and Non-Basic Substrates of Carboxypeptidase B
5. The Kinetics of Carboxypeptidase B Activity
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1. Mechanistic implications of cyanide binding to carboxypeptidase B;International Journal of Peptide and Protein Research;2009-01-12
2. Purification and partial characterization of a neutral protease from a virulent strain of Bacillus cereus;The International Journal of Biochemistry & Cell Biology;1998-05
3. Ostrich (Struthio camelus) carboxypeptidase B: Purification, kinetic properties and characterization of the pancreatic enzyme;The International Journal of Biochemistry & Cell Biology;1996-05
4. A reinvestigation of the hydration numbers of paramagnetic metalloenzymes by proton and deuteron NMR relaxation times;Journal of Magnetic Resonance (1969);1984-02
5. Metal ion effects on target sites of modification in metallocarboxypeptidase B;Journal of Inorganic Biochemistry;1983-06
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