Therapeutic potential of monteplase in acute myocardial infarction.

Thrombolysis with conventional thrombolytic agents prior to percutaneous coronary intervention (PCI) has had no impact on the treatment of acute myocardial infarction (AMI). However, the development of mutant tissue type plasminogen activators (mt-PA) has prompted us to reassess the combination of thrombolysis and PCI. Monteplase is a newly developed mt-PA that can be administered as a single intravenous bolus injection.

Long-term benefits of monteplase before coronary angioplasty in acute myocardial infarction.

Patients with acute myocardial infarction were randomly assigned to receive direct percutaneous coronary intervention (PCI) or pretreatment with intravenous monteplase followed by PCI. Although the combination of monteplase and PCI did not alter mortality compared with direct PCI, there was a dramatic reduction in the cardiac event rate over a 2-year follow-up compared with direct PCI.

Therapeutic potential of monteplase in acute myocardial infarction as a powerful thrombolytic agent for pretreatment of coronary intervention.

Thrombolysis with conventional thrombolytic agents followed by percutaneous coronary intervention (PCI) had no impact on the treatment of acute myocardial infarction (AMI). However, the development of mutant type plasminogen activator (mt-PA) has prompted us to reassess the combination of thrombolysis and PCI. Monteplase (Eisai, Co.

Mapping of functional sites on the primary structure of the contractile tail sheath protein of bacteriophage T4 by mutation analysis.

In order to determine the functional roles of amino acid residues in gp18 (gp: gene product), the contractile tail sheath protein of bacteriophage T4, the mutation sites and amino acid replacements of available and newly created missense mutants with distinct phenotypes were determined. Amber mutants were also utilized for amino acid insertion by host amber suppressor cell strains. It was found that mutants that gave rise to a particular phenotype were mapped in a particular region along the polypeptide chain.