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  • Bronchopulmonary dysplasia  (1)
  • EnterotoxigenicEscherichia coli  (1)
  • 1
    ISSN: 1432-1076
    Keywords: Respiratory distress syndrome ; Surfactant replacement ; Bronchopulmonary dysplasia ; Intraventricular haemorrhage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We conducted a prospective, randomized, controlled trial comparing the efficacy of two doses of a reconstituted bovine surfactant (Surfactant TA) in premature infants requiring mechanical ventilation shortly after birth for respiratory distress syndrome. Forty-six infants weighing 1000–1499 g were randomized into two groups: a low-dose group (23 infants given a single dose of 60 mg surfactant lipid/kg) and a high-dose group (23 infants given a single dose of 120 mg/kg). The mean (SD) age at which surfactant was given was 5.5 (±1.2) h in the low-dose group and 6.0 (±1.5) h in the high dose group. Both treatments improved oxygenation (increased arterial-alvcolar PO2 ratio) with decreased mean airway pressure, the high-dose surfactant having a more beneficial effect in prolonging the response. Infants in the high-dose group had significantly less (P〈0.05) incidence of both intraventricular haemorrhage and bronchopulmonary dysplasia. This prospective trial documents that a greater benefit can be obtained by increasing the dose of surfactant (120 mg/kg) beyond 60 mg/kg in the treatment of premature infants with severe respiratory distress syndrome (RDS).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-7284
    Keywords: EnterotoxigenicEscherichia coli ; Yibrio cholerae ; LT ; CT
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract It was examined where a protease purified from Vibrio cholerae might nick the heat-labile enterotoxin (LT) A subunit from enterotoxigenicEscherichia coli. LT was digested by the protease and contained a fragment which had the same mobility on SDS-PAGE as that of the Al fragment of LT digested by trypsin. The biological activity of LT by this protease was also identical to that of LT by trypsin. The amino acid sequence of the N-terminus of the A2-like fragment was Thr-Ser-Thr-Gly, which corresponded to the sequence from 193 to 196 of the A subunit. These data suggest that this protease, like trypsin, nicks arginine at position 192 from the N-terminus of the A subunit and that the biological activation of LT by this protease is similar to that by trypsin.
    Type of Medium: Electronic Resource
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