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Amikacin

Sample material Serum or plasma (EDTA, citrate, heparin or oxalate). If penicillin or similar substances are present, the concentration of amikacin may diminish if the sample is stored for a prolonged period. [Pg.559]

Specificity Gentamycin, neomycin, vancomycin, streptomycin and tetracycline show an error of 5% if added in a concentration of 100 mg/1 to a sample containing 15 mg/1 amikacin. [Pg.560]

Kanamycin will result in a 25% error at a concentration of 4 mg/1 and tobramycin in an error of the same magnitude at 200 mg/1 if these substances are added to a sample containing 15 mg/1 amikacin. [Pg.560]

Interferences Mild haemolysis or lipaemia will not disturb the measurement. Strong haemolysis will interfere. [Pg.560]

Patient samples containing antibodies to Escherichia coli do not produce any interference. However, in rare cases clumping may occur when the conjugate is added. This results in a concentration reading that is too low. [Pg.560]


A Acetylation, O-Phosphorylation, and O-Adenylylation. A/-Acetylation, O-phosphorjiation, and O-adenyljiation provide mechanisms by which therapeutically valuable aminocyclitol antibiotics, eg, kanamycia [8063-07-8] gentamicin [1403-66-3] sisomicin [32385-11-8], streptomycia [57-92-1], neomycin, or spectinomycin are rendered either partially or completely iaactive. Thus, eg, kanamycia B [4696-78-8] (50) can be iaactivated by modification at several sites, as shown. The elucidation of these mechanisms has allowed chemical modification of the sites at which the iaactivation occurs. Several such bioactive analogues, eg, dibekacia and amikacin have been prepared and are not subject to the iaactivation hence, they inhibit those organisms against which the parent antibiotics are iaeffective (96) (see Antibacterial agents, synthetic). [Pg.314]

Aminoglycosides. Antibiotics ia the amiaoglycoside group characteristically contain amino sugars and deoxystreptamiae or streptamiae. This family of antibiotics has frequentiy been referred to as aminocyclitol amiaoglycosides. Representative members are streptomycia, neomycin, kanamycia, gentamicin, tobramycia, and amikacin. These antibiotics all inhibit proteia biosynthesis. [Pg.474]

General Antibacterial Properties. In the clinical control of bacterial infectious disease, the aminoglycosides gentamicin, tobramycin, amikacin, netilmicin, and to a lesser extent, dibekacin and isepamicin are most commonly used for the treatment of serious infections involving aerobic or facultative gram-negative baciUi, especially in the compromised host. This usage is discussed in the Hterature (44—51). [Pg.481]

N-ethyl kanamycin A (153) has some resistance to APH(3 ), ANT(2 ), and AAC(3). Butakacin [59733-86-7] C22H N 0 2 t i l-A/-(3)-2-hydroxy-4-aminobutyl derivative of kanamycin A (154), has antimicrobial properties similar to amikacin. A similar effect was seen with the l-A/-(l,3-dihydroxy-2-propyl) derivative of kanamycin B, propikacin [66887-96-5] C22H42N 022 (155). Methylation of the 6 -amine reduces susceptibility to AAC(6 ) (156). [Pg.484]

Estimated worldwide sales are given in Table 1 for the aminoglycoside derivatives most commonly used in medicine. Although amikacin has somewhat higher sales, gentamicin is by far the most widely used in terms of number of courses of treatment. [Pg.485]

Dantrolene sodium L-(-) - y-Amino-a-hydroxybutyric acid Amikacin... [Pg.1612]

Enzymes transferring an acetyl moiety to one specific of several amino-groups of the aminocyclitol-aminoglycoside antibiotics (e.g. gentamicin, amikacin, kanamycin) are called aminoglycoside acetyltransferases... [Pg.104]

The aminoglycosides include amikacin (Amikin), gentamicin (Garamycin), kanamycin (Kantrex), neomycin (Mycifradin), netilmicin (Netromycin), streptomycin, and tobramycin (Nebcin). [Pg.93]


See other pages where Amikacin is mentioned: [Pg.40]    [Pg.40]    [Pg.40]    [Pg.178]    [Pg.479]    [Pg.480]    [Pg.481]    [Pg.481]    [Pg.481]    [Pg.482]    [Pg.482]    [Pg.482]    [Pg.483]    [Pg.483]    [Pg.484]    [Pg.484]    [Pg.485]    [Pg.57]    [Pg.57]    [Pg.58]    [Pg.59]    [Pg.1620]    [Pg.1672]    [Pg.1672]    [Pg.1672]    [Pg.1677]    [Pg.1679]    [Pg.1680]    [Pg.1710]    [Pg.1713]    [Pg.1724]    [Pg.92]    [Pg.92]    [Pg.92]    [Pg.92]    [Pg.93]    [Pg.93]    [Pg.93]    [Pg.93]    [Pg.94]    [Pg.98]    [Pg.88]   
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