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This research investigates the substrate specificity and activity of plasminogen activator in the absence of its natural substrate, plasminogen.

Limited cleavage of cellular fibronectin by plasminogen activator purified from transformed cells.

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Randomized trial explores plasminogen-free cleavage of fibronectin in transformed chicken cells, suggesting specific substrates for PA.

This research investigates the substrate specificity and activity of plasminogen activator in the absence of its natural substrate, plasminogen.
Purified plasminogen activator was incubated with potential substrates, including fibronectin and chicken ovalbumin.
Cleavage products were analyzed using polyacrylamide gels under reducing and non-reducing conditions.
Monoclonal antibodies targeting avian PA were employed to assess inhibition of fibronectin cleavage.
Fibronectin underwent limited cleavage by PA, disrupting the dimeric molecule but not affecting chicken ovalbumin.
Cleavage occurred near the carboxyl terminus and on the amino-terminal side of the interchain disulfide bridge.
Urokinase also cleaved fibronectin in plasminogen-free conditions, producing a limited range of high molecular weight products.

Quigley et al. (1987) studied this question.

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