Unknown

Dataset Information

0

Concanavalin A, a receptor protein with apparently co-operative binding characteristics.


ABSTRACT: Laser nephelometry is a suitable technique for the quantitative determination and differentiation of both lectins and glycoconjugates in the low-picomolar range. Simultaneously this method renders possible investigations on the specificity and mode of interaction between lectins and different ligands. The results demonstrate that the degree of co-operativity between concanavalin A and the respective glycoconjugate is dependent on the presence of hydrophobic binding sites and can be substantially altered by conformational changes of the ligand. The transition from apotransferrin to Fe3+-transferrin induces a transformation of the sigmoidal-shaped binding curve to a hyperbolic one. Hence, at low concentrations, Fe3+-transferrin is bound far better than apotransferrin, whereas maximal binding is nearly identical. After removal of N-acetylneuraminate, concanavalin A is less efficient in differentiating between the Fe3+-charged and Fe3+-free (apo) forms of transferrin.

SUBMITTER: Kottgen E 

PROVIDER: S-EPMC1162652 | biostudies-other | 1981 Mar

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1177774 | biostudies-other
| S-EPMC2626182 | biostudies-literature
| S-EPMC1165455 | biostudies-other
| S-EPMC3800043 | biostudies-other
| S-EPMC3339874 | biostudies-other
| S-EPMC1132805 | biostudies-other
| S-EPMC10592737 | biostudies-literature
| S-EPMC6824935 | biostudies-literature
| S-EPMC5038384 | biostudies-literature
| S-EPMC3458525 | biostudies-literature