Griaznova N S, Taisova A S, Petiushenko R M
Antibiot Med Biotekhnol. 1985 Sep;30(9):657-62.
A substance inhibiting the activity of aminoglycoside-3-'-phosphotransferases of both the actinomycetous and the bacterial origin was detected in the filtrates of the culture fluid and mycelium of Micromonospora sp. producing sisomicin. The activity of the substance against the aminoglycoside inactivating enzymes of different types was studied. It was shown that the quantity of the inhibitor in the culture fluid of Micromonospora sp. correlated with intensity of sisomocin production. Under conditions not providing production of the antibiotic the inhibitory activity was lacking. The inhibitor was purified by ion exchange chromatography on Amberlite CG-50 and KM-cellulose (NH+4 form), gel filtration through Sefadex G-50 and preparative paper chromatography. Stability of the inhibitor at different pH values and different temperatures, its sensitivity to certain enzymes and behaviour in high voltage electrophoresis were studied. The results of ultrafiltration showed that the molecular weight of the inhibitor was relatively low: less than 1000 D.
在产生西索米星的小单孢菌属的培养液滤液和菌丝体中，检测到一种能抑制放线菌来源和细菌来源的氨基糖苷-3'-磷酸转移酶活性的物质。研究了该物质对不同类型氨基糖苷失活酶的活性。结果表明，小单孢菌属培养液中抑制剂的量与西索米星的产生强度相关。在不产生抗生素的条件下，不存在抑制活性。通过在Amberlite CG-50和KM-纤维素（NH₄⁺型）上进行离子交换色谱、通过Sephadex G-50进行凝胶过滤以及制备性纸色谱对抑制剂进行了纯化。研究了抑制剂在不同pH值和不同温度下的稳定性、对某些酶的敏感性以及在高压电泳中的行为。超滤结果表明，抑制剂的分子量相对较低：小于1000 D。
