作者: A. Raz , P. Carmi , G. Pazerini
DOI:
关键词: Chimeric gene 、 Protein primary structure 、 CD69 、 Galactoside binding 、 Peptide sequence 、 Gene product 、 Biology 、 Biochemistry 、 Molecular biology 、 Homology (biology) 、 Nucleic acid sequence
摘要: Abstract We report the complete primary and secondary structures of a metastasis-associated M r 34,000 galactoside-binding lectin. The polypeptide sequence (264 amino acids) was derived from nucleotide three overlapping complementary DNA clones isolated λgt11 λgt10 phage libraries UV-induced murine fibrosarcomas. Striking features are two distinct regions β-sheet globular at carboxy terminals, respectively. Homology search suggests that is chimeric gene product formed by fusion 5′-end an ∼14,000 lectin with internal domain collagen α gene. Enzymatic treatment collagenase confirmed presence collagen-like structure in polypeptide. Unexpectedly, entire >85% homologous to rat low affinity IgE-binding protein.