title: Heparin-binding lectin from human placenta: further characterization of ligand binding and structural properties and its relationship to histones and heparin-binding growth factors.
abstract: We have previously demonstrated that the heparin-binding lectin of human placenta dissociates into up to four distinct polypeptides with molecular weights of 14,400, 15,000, 16,200, and 16,700 (Kohnke-Godt, B., & Gabius, H.-J. (1989) Biochemistry 28, 6531-6538). Stable complexes to ligands can shift the molecular weight appearance of the lectin to higher values. They can be dissociated in the additional presence of 9 M urea or by enzymatic degradation of heparin in model studies. The binding of heparin is rather stable over a range of salt concentrations from 1 to 3 M NaCl. Chemical modification with group-specific reagents to arginine, lysine, histidine, tyrosine, and tryptophan results in substantial inactivation of binding activity. Further amino-terminal sequence analyses point to a high-scoring relationship in this region to histone sequences, namely, histone H2B, but to no published sequences for any heparin-binding growth factor. Calculation of relatedness on the basis of differences in amino acid composition corroborates the conclusion of molecular distinction between the lectin, histones H2A and H2B, and the fibroblast growth factor as well as angiogenin. Histones only weakly agglutinate type II erythrocytes in contrast to the lectin. The immobilized lectin exhibits two classes of binding sites with KD values of 3 and 110 nM in contrast to one estimated KD value of 250 nM with a commercially available histone fraction. Both fractions retain binding activity to biotinylated heparin in transblots and are immunologically cross-reactive to antibodies, raised against the lectin as antigen. Subcellular fractionation clearly demonstrates that heparin-inhibitable hemagglutination activity and immunologically cross-reactive protein bands, characteristic for the lectin, but not unequivocally distinguishable from certain histone fractions in blots, are not confined to the nuclear fraction in the human placenta.
authors.affiliation: Max-Planck-Institut für Experimentelle Medizin, Abteilung Chemie, Göttingen, FRG.
authors.forename: B
authors.initials: B
authors.lastname: Kohnke-Godt
authors.forename: H J
authors.initials: HJ
authors.lastname: Gabius
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005346:Fibroblast Growth Factors / Q000737:chemistry; D006384:Hemagglutination; D006493:Heparin / Q000378:metabolism*; D006657:Histones / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010920:Placenta / Q000378:metabolism*; D011247:Pregnancy; D012689:Sequence Homology, Nucleic Acid; D013347:Subcellular Fractions / Q000378:metabolism
chemical_list: D006657:Histones; D037102:Lectins; D008024:Ligands; D005346:Fibroblast Growth Factors; D006493:Heparin