Endogenous Lectins of Bovine Pancreas

Abstract

Affinity chromatography of salt and detergent extracts from bovine pancreas on gly-. cosylated or glycoprotein-linked Sepharose 4B resulted in purification of different carbohydratebinding proteins.Three species of proteins with molecular masses of 16 kDa, 35 kDa and 64 kDa exhibiting specificity for ß-galactosides, but none with preferential specificity for a-galactosides, were isolated from salt and detergent extracts. No Ca 2 ® was required for binding.Mannan-binding proteins of 37 kDa, 47 kDa and 94 kDa without Ca 2e -requirement were only found in the salt extract. No other mannan-binding activity could be detected. Fucose-binding proteins of 34 kDa, 62 kDa and 70 kDa exhibiting Ca 2 *-requirement for binding were present in the salt extract and two proteins with 62 kDa and 70 kDa in detergent extract. The different fractions showed agglutination activity when assayed with rabbit erythrocytes. Thus they can be defined as lectins.

Isolation and Immunochemical Study of a Soluble Cerebellar Lectin Delineating Its Structure and Function

“…More recently, these compounds have been discovered in animals, including mammals (for exhaustive review, see Barondes, 198 1, 1984;Harford, 1982: Olden et al, 1982). Various lectins have been isolated from liver and macrophages (Stahl et al, 1976(Stahl et al, , 1978Kawasaki et al, 1978;Steer and Ashwell, 1980;Stockert et al, 1980;Sahagian et al, 198 1 ;Maynard and Baenziger, 1982;Mori et al, 1983;Wild et al, 1983;Gabius et al, 1984;Roche et al, 1985). It has been suggested that proteins with carbohydrate binding properties of different specificities exist in the CNS (Kobiler and Barondes, 1977;Simpson et al, 1977;Gremo et al, 1978).…”

Controlled Cell Attachment, Using Plasma Deposited Polymer Microstructures: A Novel Study of Cells‐Substrate Interactions

“…In contrast to this, human rhabdomyosarcoma cells revealed Ca 2+ ‐independent adhesion 38. Accordingly they adhere both on the pp‐AAc layers and on the hydrophobic CHF 3 plasma layers.…”

Fine-tuning of prototype chicken galectins: structure of CG-2 and structure–activity correlations

“…As provided therein, the sequence of the full-length cDNA including the first exon (two amino acids; methionine and alanine) is identical to the respective GenBank entries XM_00123499.2 (mRNA) and XM_00123499.2 (protein) and is also completely in line with the genomic sequence (Gene ID 425107). Following purification by affinity chromatography on lactosylated Sepharose 4B as a crucial step, controls for purity and activity assays were performed as described elsewhere (Gabius et al, 1984;Kaltner et al, 2008;Amano et al, 2012;André et al, 2012). Production and quality controls of CG-1A, Sequence alignment of CG-2 with (a) those of human galectin-1 and galectin-2 (hGal-1 and hGal-2) and (b) those of the other two prototype CGs (CG-1A and CG-1B).…”