The morphology of L-fucose, D-mannose specific lectin (SFL 100-2) produced by Streptomyces No. 100-2.
The morphology of an L-fucose specific lectin, SEL 100-2, from a Streptomyces sp. was studied. Electron microscopic observation showed that purified SFL 100-2 preparation consisted of particles homogeneous in size. The diameter was 25 nm. The digitized images of these particles had 2-fold rotation symmetry. The sedimentation coefficient (s020,w) was determined to be 20.6S. The particle weight and the Stokes radius were calculated to be 8.0 X 10(5) daltons and 94 A, respectively, by three independent methods, i.e., gel filtration, sedimentation equilibrium and velocity measurements. The frictional ratio (f/fmin) was estimated to be 1.53. These values are quite similar to those of human alpha 2-macroglobulin. 125I-Labeled peptide mapping indicated that these particles were built up of about twelve identical subunits (Mr = 68,000). The size of SFL 100-2 in culture broth was found to be the same as that of the particles in the purified preparations. The shape and other properties of SFL 100-2 are discussed and compared with those of the tail of lambda phage and type 1 pili of Escherichia coli, whose amino acid compositions were quite similar to that of SFL 100-2 and also those of L-fucose specific plant lectins.
D001345:Autoradiography; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D005643:Fucose; D037102:Lectins; D008358:Mannose; D008854:Microscopy, Electron; D008970:Molecular Weight; D010316:Particle Size; D010446:Peptide Fragments / Q000032:analysis; D013302:Streptomyces; D014461:Ultracentrifugation
D037102:Lectins; D010446:Peptide Fragments; C027112:fucose-binding lectin; D005643:Fucose; D008358:Mannose