Taisova A S, Griaznova N S
Antibiotiki. 1984 Sep;29(9):649-53.
Stability of aminoglycoside phosphotransferases, adenylyltransferases and acetyltransferases isolated from various sources was studied. The enzymes were characterized by different substrate profiles. They were stored at a temperature of -10 degrees C in the form of frozen solutions or at a temperature of 4 degrees C in the lyophilized form. It was shown that lyophilization markedly increased the stability of the enzymes inactivating aminoglycoside antibiotics. Aminoglycoside phosphotransferases and adenylyltransferases with streptomycin as substrate were less stable than aminoglycoside phosphotransferases with neomycin as substrate. Aminoglycoside acetyltransferases from Streptomyces fradiae 918 producing neomycin were least stable among the enzymes studied. Lyophilized enzymes as a possible stabilizer of ATP added to the preparations had no significant effect on their stability during storage.
研究了从各种来源分离得到的氨基糖苷磷酸转移酶、腺苷酸转移酶和乙酰转移酶的稳定性。这些酶具有不同的底物谱。它们以冷冻溶液的形式保存在-10℃，或以冻干形式保存在4℃。结果表明，冻干显著提高了使氨基糖苷类抗生素失活的酶的稳定性。以链霉素为底物的氨基糖苷磷酸转移酶和腺苷酸转移酶比以新霉素为底物的氨基糖苷磷酸转移酶稳定性差。在所研究的酶中，来自产生新霉素的弗氏链霉菌918的氨基糖苷乙酰转移酶稳定性最差。冻干酶作为添加到制剂中的ATP的可能稳定剂，在储存期间对其稳定性没有显著影响。
