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. 1998 Apr 6;141(1):255–265. doi: 10.1083/jcb.141.1.255

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Radiolabeled laminin-5 was captured by the laminin-5 γ2 chain antibody GB3 from the conditioned medium of pp126 cells. One sample was left untreated, whereas the other was digested with 1 μg/ml plasmin for 90 min. Approximately 2 μg of both preparations were then processed for SDS-PAGE and then the gel dried and was exposed to film. Note that the untreated material consists of three prominent polypeptides of 190-, 145- and 105-kD molecular weight (the α, β and γ chains of laminin-5, respectively), whereas in the plasmin-modified material there are major polypeptides of 160 (processed α3 subunit, indicated as α3*), 145, and 100 kD. Note that there is a minor amount of the 190-kD unprocessed α subunit in the plasmin-modified preparation. Molecular weights are indicated to the left of the gel profiles.