Lectin from Helix pomatia

Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. These oligomeric proteins are characterized by the presence of a carbohydrate recognition domain.

Lectin from Helix pomatia has been used to study its binding activities in Gyrodactylus derjavini parasitizing fins of Oncorhynchus mykiss.

Lectin is useful in glycoconjugate characterizing, imaging and targeting. Lectin participates in host recognition and tissue adhesion. Lectins shows resistance to proteolytic degradation in vivo.

HPA has anti-A human blood group specificity and has an affinity for terminal N-acetyl-α-D-galactosaminyl residues. Conjugates are prepared from affinity purified lectin.

Where reported, agglutination activity is expressed in μg/ml and is determined from serial dilutions in phosphate buffered saline, pH 6.8, of a 1 mg/ml solution. This activity is the lowest concentration to agglutinate a 2% suspension of human blood group A erythrocytes after 1 hour incubation at 25 °C.