-transparent.png){kind=logo}
The effects of ligand binding on antibody complex formation of Lactobacillus casei dihydrofolate reductase have been investigated. Binary complexes containing either substrate and inhibitors or NADP+ and NADPH together with ternary complexes containing inhibitors and coenzyme were examined. Whereas substrate and inhibitor binding alone show no effect, the binding of coenzyme reduces antibody complex formation. The most striking effect is observed with ternary complexes containing methotrexate or aminopterin and NADPH: maximal retention of the labeled protein in the immunoprecipitation assay is reduced to approximately 30% of its original value with dihydrofolate reductase alone due to a decrease in both the affinity and lifetime of the antibody-protein complex at one or more antigenic sites. This result is discussed in terms of different conformational changes brought about by NADP and NADPH.
A M Gronenborn, and
P Papadopoulos, and
G M Clore
March 1972,
Biochemistry,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
June 1996,
European journal of biochemistry,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
February 1984,
The Biochemical journal,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
December 1981,
The Journal of biological chemistry,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
February 1979,
The Biochemical journal,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
May 1979,
The Journal of biological chemistry,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
February 1982,
Biochimica et biophysica acta,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
February 1982,
Gene,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
April 1989,
Biochemical Society transactions,
A M Gronenborn, and
P Papadopoulos, and
G M Clore
February 1982,
Biochemistry,
