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  • 1
    ISSN: 1573-742X
    Keywords: saruplase ; urokinase ; pharmacokinetics ; hemostasis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The aim of the study was to compare in a single trial, using identical methodology, the pharmacokinetic properties and the effect on the hemostatic system of saruplase (unglycosylated scu-PA) and urokinase (glycosylated tcu-PA). Twenty-four patients with an acute myocardial infarction were either treated with saruplase (n = 12; 20 mg IV bolus followed by a 60 mg infusion for 60 minutes) or urokinase (n = 12; 1.5 million IU IV bolus followed by 1.5 million IU infusion for 60 minutes). Blood samples from saruplase-treated patients were analyzed for u-PA antigen and total u-PA and tcu-PA activities; those from urokinase-treated patients for u-PA antigen and tcu-PA activity. The effect of treatment on, including recovery of, plasma α2-antiplasmin, fibrinogen, and plasminogen was examined in both groups. The total clearance of urokinase (179 ± 55 ml/ min) is about half that of saruplase (406 ± 154 ml/min), and the mean residence time of urokinase (59.1 ± 22.5 minutes) is nearly twice that of saruplase (28.3 ± 7.8 minutes), which results in a slower elimination of urokinase from plasma. Whether differences in the pharmacokinetic behavior of the unglycosylated saruplase and the glycosylated urokinase observed in this study are due to the difference in glycosylation or to other factors is not resolved. The systemic effect of saruplase on α2,-antiplasmin, fibrinogen, and plasminogen is similar to that of urokinase, although retarded.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 203 (1986), S. 177-184 
    ISSN: 1617-4623
    Keywords: Hafnia alvei ; Lysine decarboxylase ; Gene cloning ; DNA sequence analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A lysine decarboxylase (LDC) gene from Hafnia alvei was cloned in the Escherichia coli strain HB101. A gene bank consisting of 2,000 clones, carrying recombinant plasmids with large DNA fragments of H. alvei integrated in the BamH1 site of pBR322, was screened for LDC activity by a colony filter radioimmunoassay. The gene bank yielded clone 462 expressing high LDC activity with the presence of a plasmid carrying a 7.5 kb insert of H. alvei. Two LDC-positive subclones derived from 462 with inserts of 2.9 and 3.3 kb were sequenced by the shotgun method. An open reading frame for a 83 K protein with 739 amino acids was determined as the coding region for the LDC. The identification of this reading frame as the true reading frame of the H. alvei LDC gene and its similarities with LDC of E. coli are described. The use of the cloned gene for the transformation of plant cells is discussed.
    Type of Medium: Electronic Resource
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