Human laminin isolated in a nearly intact, biologically active form from placenta by limited proteolysis.
作者： U Wewer , R Albrechtsen , M Manthorpe , S Varon , E Engvall
DOI: 10.1016/S0021-9258(17)44226-8
关键词:
摘要: A protein with properties of laminin has been isolated from human placental extracts by using monoclonal antibodies. Placental tissue was extracted 0.5 M NaCl and high molecular weight proteins were the extract salt precipitation gel filtration on Sepharose 6B. The resulting fraction which contained material cross-reactive anti-sera to rat used as immunogen prepare hybridomas. Thirteen hybrids produced antibodies reacted basement membrane-associated antigens in indirect immunofluorescence tissues. One these, 4E10, characterized detail. This antibody shown several lines evidence. Immunoprecipitation metabolically labeled culture media a amniotic epithelial cell line 4E10 followed sodium dodecyl sulfate-polyacrylamide electrophoresis revealed polypeptides Mr similar those laminin. Immunochromatography obtained limited pepsin digestion yielded main at 160 130 kilodaltons after reduction. These peptic fragments cross-reacted immunodiffusion enzyme immunoassay, polyclonal antiserum against membranes tissues manner identical antibody. Electron microscopic images showed structures cross-shaped murine laminins, although short arms truncated various degrees or even absent. also displayed biological activity that laminins outgrowth neurites neuronal cells promoted plates coated fragments.
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