The 18O isotope effect in 13C nuclear magnetic resonance spectroscopy: mechanistic studies on asparaginase from Escherichia coli.

[1]  K. Röhm,et al.  Stereospecific synthesis of L‐[1,4‐13C2]aspartic acid, L‐β‐([13C]cyano)alanine and L‐[4‐13C]aspartic acid , 1985 .

[2]  J. Parente,et al.  18O isotope effect in 13C nuclear magnetic resonance spectroscopy. IX: Hydrolysis of benzyl phosphate by phosphatase enzymes and in acidic aqueous solutions , 1984 .

[3]  I. Knack,et al.  Microcomputers in enzymology. A versatile BASIC computer program for analyzing kinetic data. , 1981, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

[4]  J. Risley,et al.  /sup 18/O-isotope effect in /sup 13/C nuclear magnetic resonance spectroscopy. 4. Oxygen exchange of (1-/sup 13/C, /sup 18/O/sub 2/)acetic acid in dilute acid , 1981 .

[5]  R. Handschumacher,et al.  Synthesis of model compounds relevant to the active-site-directed inactivation of L-asparaginase by 5-diazo-4-oxo-L-norvaline. , 2009, International journal of peptide and protein research.

[6]  J. Risley,et al.  /sup 18/O isotope shift upon /sup 13/C NMR spectra and its application to the study of oxygen exchange kinetics , 1979 .

[7]  R. Handschumacher,et al.  Structure of peptide from active site region of Escherichia coli L-asparaginase. , 1977, The Journal of biological chemistry.

[8]  Y. Tamaura,et al.  Modification of cystine or tryptophan residues in the asparaginase molecule and their role in conformation and antigenicity , 1976, FEBS letters.

[9]  L. Jaenicke,et al.  Untersuchungen an der L-Asparaginase, Inaktivierung und Modifizierung des Enzyms durch N-Bromsuccinimid und Substratspezifität der Reaktion , 2009 .

[10]  K. Röhm,et al.  On the substrate specifity of l‐asparaginase from E. coli , 1974, FEBS letters.

[11]  R. Homer.  The pH dependence and quenching of the fluorescence of asparaginase from Escherichia coli B. , 1972, Biochimica et biophysica acta.

[12]  N. Kitron,et al.  Stereospecific features of the conformative response of L-asparaginase. , 1972, Biochemistry.

[13]  J. H. Schwartz,et al.  L-asparaginase II of Escherichia coli. Studies on the enzymatic mechanism of action. , 1971, The Journal of biological chemistry.

[14]  R. Jackson,et al.  Escherichia coli L-asparaginase. Catalytic activity and subunit nature. , 1970, Biochemistry.

[15]  H. Bergmeyer.  Methods of Enzymatic Analysis , 2019 .

[16]  I. Page,et al.  Synthesis of a Biologically Active Octapeptide Similar to Natural Isoleucine Angiotonin Octapeptide1 , 1957 .