Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pregnancy zone protein (PZP, alpha 2-PAG, SP3) was found to bind to plasmin in crossed affino-immunoelectrophoresis using sodium caseinate in the first dimension gel. The plasmin presence in the PZP-plasmin complex was confirmed by addition of antiserum against plasminogen to the gel. In crossed affino-immunoelectrophoresis using plasmin in the first dimension gel a non migrative PZP immunoreactive peak appeared, similar to the peak obtained with casein in the first dimension gel. Incubation of mixtures of PZP and plasmin also demonstrated complex formation between PZP and plasmin. The complex between PZP and plasmin could be precipitated not only by anti-PZP antibodies, but also by anti-plasminogen antibodies, confirming the interaction between the two molecules. The significance of the binding between plasmin and PZP remains to be elucidated, but it is tempting to speculate that PZP, present on the trophoblastic surface, immobilizes plasmin, rendering this molecule able to perform a local fibrinolytic activity.
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PMID:Interaction between pregnancy zone protein and plasmin. 297 40

Human fibrinogen exposed to 46.5 degrees C was subjected to gel permeation chromatography. The protein eluted in two distinct peaks. The first peak appeared in the void volume containing soluble fibrinogen aggregates, while the other peak represented monomeric fibrinogen. In contrast to the monomeric peak material, the aggregate fraction reacted with a panel of monoclonal antibodies specific for fragment D-dimer using an ELISA system. Edman degradation showed that both the aggregate and the monomeric fractions were devoid of soluble fibrin, and immunoblots of SDS-PAG electrophoretic profiles disclosed no sign of stabilized high molecular weight derivatives. We have previously shown that the aggregate fraction of similarly treated fibrinogen, in contrast to the monomeric fraction, stimulates the t-PA catalyzed conversion of plasminogen to plasmin and concomitantly exposes the sequences Aalpha-(148-160) and gamma-(312-324) involved in t-PA stimulation. Our present and previous findings suggest that soluble fibrinogen aggregates possess a fibrin-like structure, and that fibrin or fibrinogen polymer formation is a prerequisite for the enhancing effect on t-PA-mediated plasminogen to plasmin conversion which is seen even with the polymers in the soluble state.
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PMID:D-dimer specific monoclonal antibodies react with fibrinogen aggregates. 916 70