Interaction of calcium and manganese ions with apoconcanavalin A and sugar binding.

@article{Harrington1978InteractionOC,
  title={Interaction of calcium and manganese ions with apoconcanavalin A and sugar binding.},
  author={P. C. Harrington and R. G. Wilkins},
  journal={Biochemistry},
  year={1978},
  volume={17 20},
  pages={
          4245-50
        }
}
The interaction of apoconcanavalin A (apo-Con A) with Mn2+ and Ca2+ was studied at 25 degrees C using fluorescence stopped flow. The reaction was monitored using 4-methylumbelliferyl alpha-D-mannopyranoside whose fluorescence is quenched on binding to the metalloproteins. At pH 5.0 entry of Mn2+ into apo is second-order (rate constant = 1.2 x 103 M(-1) s(-1)); at higher pH the rate constant is greater than 104 M(-1) s(-1). Reaction of excess Ca2+ with Mn(Con A) is pseudo-first-order with kobsd… Expand
Thermodynamics of metal cation binding to apoconcanavalin A
Abstract The thermodynamics of the binding of Mn +2 , Co +2 , Ni +2 , Zn +2 , and Cd +2 to demetallized concanavalin A (apoCon A) in 0.02 M dimethylglutaric-NaOH buffer (pH 5.0–5.8 and pH 6.9) wasExpand
Manganese, calcium, and saccharide binding to concanavalin A, as studied by ultrafiltration.
TLDR
Experiments of binding of 4-methylumbelliferyl alpha-D-mannopyranoside to concanavalin A indicated that at pH 5.2, binding of a single Mn2+ per concanvalin A monomer was sufficient to induce a fully active saccharide binding site. Expand
Role of second metal ion in establishing active conformations of concanavalin A.
TLDR
The stoichiometry of Mn2+ binding to concanavalin A was found to be influenced by temperature, pH, and the presence or absence of saccharide, and has a higher affinity for methylumbelliferyl alpha-D-mannopyranoside than Ni-Mn, Co- Mn, Zn, and Cd-Cd-concanvalin A. Expand
Stoichiometry of manganese and calcium ion binding to concanavalin A.
TLDR
It is reconfirm that, at equilibrium in the presence of excess Mn2+, the binding stoichiometry of Mn2+ to Con A is 2:1, both in the absence and presence of saccharide. Expand
Metal Ion Interactions with Apo-Concanavalin A and Some Observations on Metal Ion Requirements and Sugar Binding by Bandeiraea simplicifolia I Lectin
The kinetics of interaction of Ca2+ ions with M ConA (M = Co2+, Mn2+, Ni2+ and Zn2+) were followed by using the quenching of fluorescence of 4-methylumbelliferyl-α-D-mannopyranoside when bound toExpand
Metal ion induced conformational changes in concanavalin A: evidence for saccharide binding to one metal free structure.
TLDR
EDTA quickly removes all metal ions from the active Mn2+ or Co2+-concanavalin A samples leaving a metastable metal free structure which retains its high saccharide affinity for several hours at room temperature. Expand
Metal ion binding and conformational transitions in concanavalin A: a structure-function study.
TLDR
It appears that the transition between the two conformations of Con A involves a cis-trans isomerization of an Ala-Asp peptide bond in the backbone of the protein, near one of the two metal ion binding sites. Expand
Effects of manganese and calcium on conformational stability of concanavalin A: a differential scanning calorimetric study.
  • J. Zahnley
  • Chemistry, Medicine
  • Journal of inorganic biochemistry
  • 1981
TLDR
Investigation of the effect of degree of saturation of concanavalin A with Mn2+ or Ca2+, or both, on its thermal denaturation was investigated, consistent with intrasubunit cooperativity in metal ion-induced stabilization of concavelin A. Expand
Heparin and concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity.
TLDR
Results confirm that Ca2+ and Mn2+ can occupy both sites on Concanavalin A and activate the protein for binding heparin and point also to a crucial role of Ca2- in the binding capacity of the active heparIn fraction. Expand
Kinetic studies of the demetallization and inactivation of concanavalin A.
TLDR
The rates of dissociation of the metals from the different protein species, as measured spectrophotometrically using terpyridine, were found to be identical to the rates (k1) of loss of protein sugar binding affinity in the presence of EDTA as measured by assays with the fluorescent sugar, 4-methylumbelliferyl alpha-D-mannoside. Expand
...
1
2
3
4
...

References

SHOWING 1-10 OF 41 REFERENCES
Kinetics of formation and dissociation of metallocarboxypeptidases.
TLDR
Rate constants for dissociation of CoCPA, NiCPA, and ZnCPA were measured by loss of enzyme activity on addition of the metal ion scavenger EDTA, and values of K obtained kinetically were in good agreement with those determined by activity measurements of equilibrated solutions. Expand
Sugar binding properties of various metal ion induced conformations in concanavalin A.
TLDR
The locked form of concanavalin A is unstable at a pH near 2 and unfolds to the unlocked structure with a half-life of 25 min resulting in simultaneous loss of metal and sugar binding. Expand
Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A.
TLDR
Results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. Expand
Kinetic parameters for the binding of p-nitrophenyl α-d-mannopyranoside to concanavalin A
Abstract Binding of the chromogenic ligand p -nitrophenyl α- d -mannopyranoside to concanavalin A was studied in a stopped-flow spectrometer. Formation of the protein-ligand complex could beExpand
Binding of 4-Methylumbelliferyl α-d-Mannopyranoside to Tetrameric Concanavalin A
The kinetics of saccharide binding to the tetramer form of concanavalin A have been studied at pH 7.2 with the temperature-jump method. 4-Methylumbelliferyl α-d-mannopyranoside was used as a ligand;Expand
Calcium-induced cooperativity of manganese binding to concanavalin A.
TLDR
Observations indicate that at physiological pH the role of metal ions in determining functional properties of concanavalin A is different from that suggested by metal binding studies conducted at lower pH values. Expand
The kinetics of carbohydrate binding to concanavalin A.
  • R. Gray, R. Glew
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 1973
TLDR
The kinetics and equilibrium of binding of the chromophoric sugar derivative p-nitrophenyl-α-d-mannopyranoside to concanavalin A at pH 6.95 have been studied and are consistent with a simple association-dissociation scheme with independent sugar binding sites. Expand
Binding of 4-methylumbelliferyl alpha-D-mannopyranoside to dimeric concanavalin A: fluorescence temperature-jump relaxation study.
TLDR
The kinetics of saccharide binding to the dimer form of concanavalin A (con A) has been studied at pH 5.5 with the fluorescence temperature-jump method and the two derivatized forms of con A show almost identical carbohydrate binding parameters as the underivatized protein. Expand
Physical-chemical studies on the role of the metal ions in concanavalin A.
TLDR
Kinetic analysis and data are consistent with a suggestion by Cuatrecasasas (1973) that α-methyl- d -glucopyranoside binds to a locus different from the membrane binding (or agglutination) site. Expand
Magnetic resonance studies of concanavalin A:CONFORMATIONAL CHANGES INDUCED BY Ca2+ and alpha-methyl-D-mannopyranoside.
TLDR
Three independent solution spectroscopic techniques have been utilized to demonstrate mental ion- and monosaccharide inhibitor-induced structural perturbations for the dimeric form of the plant lectin concanavalin A (Con A). Expand
...
1
2
3
4
5
...