John A. Montgomery
Los Alamos National Laboratory
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Biochemical and Biophysical Research Communications | 1981
Lennie Cocco; Carroll Temple; John A. Montgomery; Robert E. London; Raymond L. Blakley
Summary [2- 13 C]Methotrexate bound to dihydrofolate reductase from Lactobacillus casei has been studied by nuclear magnetic resonance. The chemical shift for enzyme-bound methotrexate over the range pH 6.0 to 9.0 is constant and close to that for free, protonated methotrexate. Furthermore, the ultraviolet spectrum of bound methotrexate is the same from pH 6.4 to pH 10.0 and considerably different from that of free, unprotonated methotrexate. These data indicate that N-1 of bound methotrexate has pK > 10. From this and from the measured apparent association constants of methotrexate and folate it can be concluded that the charge interaction between the protonated N-1 of bound methotrexate and the active site carboxyl accounts for the particularly tight binding of the inhibitor.
Archive | 1980
Carroll Temple; John A. Montgomery
Archive | 1981
Carroll Temple; John A. Montgomery
Archive | 1978
Carroll Temple; Robert D. Elliott; Jerry D. Rose; John A. Montgomery
Archive | 1981
Carroll Temple; John A. Montgomery
Archive | 1983
Raymond L. Blakley; Lennie Cocco; John A. Montgomery; Carroll Temple; Barbara Roth; Susan Mary Daluge; Robert E. London
Archive | 1981
Carroll Temple; John A. Montgomery
Archive | 1981
Carroll Temple; John A. Montgomery
Archive | 1981
Carroll Temple; John A. Montgomery
Archive | 1982
Jr Carroll G Temple; John A. Montgomery; Robert D. Elliott; Glynn P. Wheeler