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阴道毛滴虫中的几丁质酶活性。

Chitinolytic activities in Trichomonas vaginalis.

作者信息

Sanon A, Bories C, Loiseau P M

机构信息

Biologie et Contrôle des Organismes Parasites, Faculté de Pharmacie, Université de Paris-Sud, Châtenay-Malabry.

出版信息

Parasite. 1998 Mar;5(1):75-8. doi: 10.1051/parasite/1998051075.

Abstract

Chitinolytic activities were identified in the Protozoa Trichomonas vaginalis. Overall chitinase activity assessed using chitine-azure as substrate was 10.93 +/- 1.21 nmoles/min/mg prot. End nonreducing chitobiosidase (exochitinase) and chitotriosidase (endochitinase) activities were shown using p-nitrophenyl-substrates and had specific activities of 4.55 +/- 0.53 and 0.47 +/- 0.06 nmol/min/mg prot, Kmapp. = 1.32 mM and 5 microM and pH optimum = 7.0 and 6.1 respectively. beta-N-acetylhexosaminidase (NAHase) activity was also detected with a specific activity of 5.40 +/- 0.65 nmol/min/mg prot., Kmapp = 0.656 mM and pH optimum at 7.0. No release of these enzymes into the culture medium was found. The possible role of chitinases in T. vaginalis remains to be investigated.

摘要

在原生动物阴道毛滴虫中发现了几丁质分解活性。以几丁质天青为底物评估的总几丁质酶活性为10.93±1.21纳摩尔/分钟/毫克蛋白。使用对硝基苯基底物显示了末端非还原壳二糖酶(外切几丁质酶)和壳三糖酶(内切几丁质酶)活性,其比活性分别为4.55±0.53和0.47±0.06纳摩尔/分钟/毫克蛋白,表观Km值分别为1.32毫摩尔和5微摩尔,最适pH值分别为7.0和6.1。还检测到β-N-乙酰己糖胺酶(NAHase)活性,比活性为5.40±0.65纳摩尔/分钟/毫克蛋白,表观Km值为0.656毫摩尔,最适pH值为7.0。未发现这些酶释放到培养基中。几丁质酶在阴道毛滴虫中的可能作用仍有待研究。

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