CYTOCHEMICAL-LOCALIZATION OF CATALASE ACTIVITY IN METHANOL-GROWN HANSENULA-POLYMORPHA
CYTOCHEMICAL-LOCALIZATION OF CATALASE ACTIVITY IN METHANOL-GROWN HANSENULA-POLYMORPHA
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DOI：
10.1007/bf00447145
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发表时间：
1975-01-01
影响因子：
2.8
通讯作者：
HARDER, W
中科院分区：
文献类型：
--
作者：
VANDIJKEN, JP;VEENHUIS, M;HARDER, W
本文用二氨基联苯胺（DAB）细胞化学染色法研究了酵母多形汉逊酵母甲醇培养细胞中过氧化物酶活性的定位。DAB的氧化产物出现在微体中，微体在甲醇中生长时形成，并出现在线粒体的胞内空间，微体的染色依赖于H_2O_2，在pH 10.5时最佳，低于pH 10时减弱，并被20 mM 3-氨基-1，2，4-三唑（AT）抑制。与这些观察结果相反，线粒体中的反应不依赖于H2O2，并且在8.5至10.5的范围内不受pH差异的显著影响。用甲醇代替H_2O_2后，微粒体和线粒体也被染色。适当的对照实验表明，在这种情况下，甲醇氧化酶产生过氧化氢的过氧化氢转化DAB。这些结果表明，过氧化氢酶位于甲醇生长的酵母的微体。一个可能的生理功能的微体在甲醇上的生长过程中提出的模型。
The localization of peroxidase activity in methanol-grown cells of the yeastHansenula polymorphahas been studied by a method based on cytochemical staining with diaminobenzidine (DAB). The oxidation product of DAB occurred in microbodies, which characteristically develop during growth on methanol, and in the intracristate space of the mitochondria.The staining of microbodies was H2O2dependent, appeared to be optimal at pH 10.5, diminished below pH 10 and was inhibited by 20 mM 3-amino 1,2,4 triazole (AT). In contrast to these observations, the reaction in the mitochondria was not H2O2dependent and not notably affected by differences in pH in the range of 8.5 to 10.5. Microbodies and mitochondria were also stained when H2O2was replaced by methanol. Appropriate control experiments indicated that in this case methanol oxidase generated the H2O2for the peroxidative conversion of DAB by catalase. These results suggest that catalase is located in the microbodies of methanol-grown yeasts. A model for a possible physiological function of the microbodies during growth on methanol is put forward.