Developmental changes in the structural organization of the lectin discoidin I detected by limited proteolysis.
Digestion of discoidin I with several proteolytic enzymes reveals the existence of structural domains in this lectin. Significative differences have been detected in the pattern of fragments generated by V8 protease on discoidin I of various developmental situations. The changes observed can be related to the presence of various types of tetrameric structures in discoidin I. Together with the presence of different types of isoforms in vegetative vs. differentiated cells, the results presented here suggest the involvement of different structural organizations in discoidin I which can be related to the biological functions of this lectin.
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Instituto de Investigaciones Biomédicas, CSIC, Madrid, Spain.
Pestaña
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Cano
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D004023:Dictyostelium / Q000254:growth & development*; D000070821:Discoidins; D005656:Fungal Proteins / Q000032:analysis*; D037102:Lectins; D010446:Peptide Fragments / Q000032:analysis; D015800:Protozoan Proteins; D012697:Serine Endopeptidases / Q000378:metabolism; D013997:Time Factors; D014357:Trypsin / Q000378:metabolism
D000070821:Discoidins; D005656:Fungal Proteins; D037102:Lectins; D010446:Peptide Fragments; D015800:Protozoan Proteins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin