scholarly journals Stopped-Flow Kinetics of the Formation and Decomposition of 2,4- and 4,4-Disubstituted Meisenheimer Complexes in the Reaction of 4-Piperidino-1,3-dinitrophenanthrene with Potassium Methoxide in Dimethyl Sulfoxide–Methanol

1989 ◽  
Vol 62 (1) ◽  
pp. 185-188 ◽  
Author(s):  
Hiroyuki Takahashi ◽  
Takao Hiraide ◽  
Yohji Hashida ◽  
Shizen Sekiguchi
Keyword(s):  
Dimethyl Sulfoxide ◽  
Stopped Flow ◽  
Potassium Methoxide ◽  
Meisenheimer Complexes ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

scholarly journals Stopped-Flow Kinetics of Reactions of 1-Ethoxy-2,4-dinitronaphthalene with Pyrrolidine and Piperidine in Dimethyl Sulfoxide Solution

1989 ◽  
Vol 62 (6) ◽  
pp. 1969-1975 ◽  
Author(s):  
Hajime Fujinuma ◽  
Masaru Hosokawa ◽  
Tohru Suzuki ◽  
Mitsuo Sato ◽  
Shizen Sekiguchi
Keyword(s):  
Dimethyl Sulfoxide ◽  
Stopped Flow ◽  
Dimethyl Sulfoxide Solution ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

scholarly journals Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies

1987 ◽  
Vol 243 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S R Patanjali ◽  
M J Swamy ◽  
A Surolia
Keyword(s):  
Amino Acid ◽  
Protein A ◽  
Stopped Flow ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Native Protein ◽  
Tryptophan Residues ◽  
Stopped Flow Kinetics ◽  
Two Phases ◽  
Kinetics Of

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

Absorbance and fluorescence stopped-flow kinetics of Rhus laccase and the catalytic reaction sequence

Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2049-2056 ◽  
Author(s):  
Finn B. Hansen ◽  
Robert W. Noble ◽  
Murray J. Ettinger
Keyword(s):  
Catalytic Reaction ◽  
Stopped Flow ◽  
Reaction Sequence ◽  
Stopped Flow Kinetics ◽  
Kinetics Of
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