TY - JOUR T1 - Purification, chemical, and immunochemical properties of a new lectin from Mimosoideae (Parkia discolor). AU - Cavada,B S, AU - Madeira SVF,, AU - Calvete,J J, AU - Souza,L A, AU - Bomfim,L R, AU - Dantas,A R, AU - Lopes,M C, AU - Grangeiro,T B, AU - Freitas,B T, AU - Pinto,V P, AU - Leite,K B, AU - Ramos,M V, PY - 2000/11/7/pubmed PY - 2001/3/3/medline PY - 2000/11/7/entrez SP - 271 EP - 80 JF - Preparative biochemistry & biotechnology JO - Prep Biochem Biotechnol VL - 30 IS - 4 N2 - A glucose/mannose-binding lectin was isolated from seeds of Parkia discolor (Mimosoideae) using affinity chromatography on Sephadex G-100 gel. The protein presented a unique component in SDS-PAGE corresponding to a molecular mass of 58,000 Da, which is very similar to that of a closely related lectin from Parkia platycephala. Among the simple sugars tested, mannose was the best inhibitor, but biantennary glycans, containing the trimannoside core, present in N-glycoproteins, also seem to be powerful inhibitors of the haemagglutinating activity induced by the purified lectin. The protein was characterised by high content of glycine and proline and absence of cysteine. Rabbit antibodies, anti-P. platycephala seed lectin, recognised the P. discolor lectin. However, no cross-reaction was observed when a set of other legume lectins from sub-family Papilionoideae and others from families Moraceae and Euphorbiaceae were assayed with the Parkia lectins. This suggests that Parkia lectins comprise a new group of legume lectins exhibiting distinct characteristics. SN - 1082-6068 UR - https://www.unboundmedicine.com/medline/citation/11065272/Purification_chemical_and_immunochemical_properties_of_a_new_lectin_from_Mimosoideae__Parkia_discolor__ DB - PRIME DP - Unbound Medicine ER -