Cloning, overexpression, and purification of aminoglycoside antibiotic nucleotidyltransferase (2'')-Ia: conformational studies with bound substrates.

Aminoglycoside nucleotidyltransferase (2'')-Ia [ANT (2'')-Ia] was cloned from Pseudomonas aeruginosa and purified from overexpressing Escherichia coli BL21(DE3) cells. The first enzyme-bound conformation of an aminoglycoside antibiotic in the active site of an aminoglycoside nucleotidyltransferase was determined using the purified aminoglycoside nucleotidyltransferase (2' ')-Ia. The conformation of the aminoglycoside antibiotic isepamicin, a psuedo-trisaccharide, bound to aminoglycoside nucleotidyltransferase (2' ')-Ia has been determined using NMR spectroscopy.

[Hemoperfusion in flecainide poisoning].

A 79-year-old patient, who had received a pacemaker after suffering two posterior myocardial infarctions, was treated with 2 X 100 mg flecainide daily for 9 days for ventricular extrasystoles (Lown IV b). On admission to the hospital the parameters of renal function were within the normal range. Ten days after flecainide treatment was begun a temporary electromechanic decoupling of the pacemaker occurred with reversible asystoly and progressive kidney failure.