BIOCHEMICAL CYTOLOGY OF TRICHOMONAD FLAGELLATES
BIOCHEMICAL CYTOLOGY OF TRICHOMONAD FLAGELLATES
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毛滴虫鞭毛虫的生化细胞学
DOI：
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发表时间：
1973
影响因子：
7.8
通讯作者：
Miklós Müller
中科院分区：
文献类型：
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作者：
Miklós Müller
为了确定胎儿三毛滴虫中几种酶的定位，将无菌 KV-1 菌株培养在含有牛血清的 Diamond 培养基中，在 0.25 M 蔗糖中均质化，并进行分析差速和等密度离心。分析这些级分的酶组成并用电子显微镜检查。 NADH 和 NADPH 脱氢酶、约 90% 的过氧化氢酶以及两种水解酶 α-半乳糖苷酶和锰激活的 β-半乳糖苷酶 I 位于细胞质的不可沉积部分。 α-甘油磷酸和苹果酸脱氢酶与大颗粒相关，其在蔗糖梯度中的平衡密度为1.24。该颗粒对应于肋旁颗粒和轴突旁颗粒的群体，其具有被单个膜包围的均匀颗粒基质，类似于来自其他生物体的微生物。过氧化氢酶的小部分可沉降部分（约占总活性的 10%）与这些颗粒不相关，并在密度 1.22 处达到平衡。无法确定携带过氧化氢酶的亚细胞实体的性质。最适 pH 值约为 6-6.5 的水解酶（蛋白酶、β-N-乙酰氨基葡萄糖苷酶、β-N-乙酰氨基半乳糖苷酶和阳离子非依赖性 β-半乳糖苷酶 II）以及大部分酸性磷酸酶与密度在 1.15 至 1.20 之间达到平衡的大颗粒群相关。这些颗粒中的水解酶在冷冻和解冻后很容易失去其结构结合潜伏期。这些颗粒对应于肋旁和轴突旁颗粒的另一群，其形状各异，含量不均匀，具有频繁的髓鞘质图形，表明具有消化功能。其余的磷酸酶和大部分酸性 β-葡萄糖醛酸酶活性处于较小的颗粒部分，平衡密度约为 1.18。这些酶的潜伏期非常耐冷冻和解冻。这种颗粒群由较小的、通常是扁平的囊泡和颗粒组成，其中许多显然是细胞中突出的高尔基体的碎片。
To determine the localization of several enzymes in Tritrichomonas foetus, the axenic KV-1 strain was grown in Diamond's medium with bovine serum, homogenized in 0.25 M sucrose, and subjected to analytical differential and isopycnic centrifugation. The fractions were assayed for their enzymatic composition and examined electron microscopically. NADH and NADPH dehydrogenases, about 90% of the catalase, and two hydrolases, α-galactosidase and manganese-activated β-galactosidase I are in the nonsedimentable part of the cytoplasm. α-Glycerophosphate and malate dehydrogenases are associated with a large particle, whose equilibrium density in sucrose gradients is 1.24. This particle corresponds to that population of the paracostal and paraxostylar granules which, having a uniform granular matrix surrounded by a single membrane, resemble microbodies from other organisms. The small sedimentable portion of catalase (about 10% of the total activity) is not associated with these granules and equilibrates at density 1.22. The nature of the subcellular entity carrying catalase could not be ascertained. Hydrolases with a pH optimum around 6–6.5 (protease, β-N-acetylglucosaminidase, β-N-acetylgalactosaminidase, and cation-independent β-galactosidase II), as well as a large part of acid phosphatase, are associated with a population of large particles which equilibrate at densities from 1.15 to 1.20. The hydrolases in these granules lose their structure-bound latency easily after freezing and thawing. These particles correspond to another population of the paracostal and paraxostylar granules which have varied shape and inhomogeneous content with frequent myelin figures, indicating a digestive function. The rest of the phosphatase and most of the acid β-glucuronidase activity are in a smaller granule fraction with an equilibrium density around 1.18. The latency of these enzymes is quite resistant to freezing and thawing. This particle population consists of smaller, very often flattened vesicles and granules, many of which are clearly fragments of the prominent Golgi apparatus of the cell.