A fluorimetric study of substrate and effector binding of D-ribulose-1,5-biphosphate carboxylase/oxygenase from spinach

Biochemical and Biophysical Research Communications

Volumn 74, Issue 4, 1977, Pages 1618-1625

  Vater, Joachim ^a   Salnikow, Johann ^a   Kleinkauf, Horst ^a  

^a TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

OXYGENASE;

6 (PARA TOLUIDINO) 2 NAPHTHALENESULFONIC ACID; IN VITRO STUDY; MODEL; PLANT; THEORETICAL STUDY;

BINDING SITES; CARBOXY-LYASES; CENTRIFUGATION, DENSITY GRADIENT; FRUCTOSEPHOSPHATES; HEXOSEDIPHOSPHATES; HEXOSEPHOSPHATES; MAGNESIUM; OXYGENASES; PLANTS; PROTEIN BINDING; RIBULOSE-BISPHOSPHATE CARBOXYLASE; RIBULOSEPHOSPHATES; SPECTROMETRY, FLUORESCENCE;

EID: 0017579903     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/0006-291X(77)90628-3     Document Type: Article

References (13)

1. Fluorescent Probes for Conformational States of Proteins. II. The Binding of 2-p-Toluidinylnaphthalene-6-sulfonate to α-Chymotrypsin*
2. Regulation of Ribulose 1,5-Diphosphate Carboxylase by Substrates and Other Metabolites: Further Evidence for Several Types of Binding Sites
3. Activation and Inhibition of Ribulose 1,5-Diphosphate Carboxylase by 6-Phosphogluconate
4. Inhibition of Ribulose 1,5-Diphosphate Carboxylase by 6-Phosphogluconate
5. Activation of Ribulose 1,5-Diphosphate Carboxylase by Nicotinamide Adenine Dinucleotide Phosphate and Other Chloroplast Metabolites