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The localization of alpha-hydroxy acid oxidase in renal microbodies.

作者信息

Allen J M, Beard M E, Kleinbergs S

出版信息

J Exp Zool. 1965 Dec;160(3):329-44. doi: 10.1002/jez.1401600310.

DOI:10.1002/jez.1401600310
PMID:4379960
Abstract
摘要

相似文献

1
The localization of alpha-hydroxy acid oxidase in renal microbodies.α-羟酸氧化酶在肾微体中的定位。
J Exp Zool. 1965 Dec;160(3):329-44. doi: 10.1002/jez.1401600310.
2
Alpha-hydroxy acid oxidase: localization in renal microbodies.α-羟酸氧化酶:在肾微体中的定位
Science. 1965 Sep 24;149(3691):1507-9. doi: 10.1126/science.149.3691.1507.
3
Preparation and characterization of catalase-positive particles ('microperoxisomes') from Harder's gland of the rat.大鼠哈德氏腺过氧化氢酶阳性颗粒(“微过氧化物酶体”)的制备与表征
Exp Cell Res. 1975 Jan;90(1):15-9. doi: 10.1016/0014-4827(75)90351-1.
4
Cytochemical localization by ferricyanide reduction of -hydroxy acid oxidase activity in peroxisomes of rat kidney.用铁氰化物还原法对大鼠肾脏过氧化物酶体中α-羟酸氧化酶活性进行细胞化学定位。
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5
The cytochemical demonstration of catalase and D-amino acid oxidase in the microbodies of teleost kidney cells.硬骨鱼肾细胞微体中过氧化氢酶和D-氨基酸氧化酶的细胞化学显示
Histochem J. 1977 Mar;9(2):171-81. doi: 10.1007/BF01003629.
6
Histochemical studies of thyroid cells in long-term tissue culture.
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7
Catalase-positive particles ("microperoxisomes") from rat preputial gland and bovine adrenal cortex.来自大鼠包皮腺和牛肾上腺皮质的过氧化氢酶阳性颗粒(“微过氧化物酶体”)。
Exp Cell Res. 1975 Jul;93(2):438-42. doi: 10.1016/0014-4827(75)90470-x.
8
Tissue fractionation studies. 18. Resolution of mitochondrial fractions from rat liver into three distinct populations of cytoplasmic particles by means of density equilibration in various gradients.组织分级分离研究。18. 通过在各种梯度中进行密度平衡,将大鼠肝脏的线粒体分级分离为三种不同的细胞质颗粒群体。
Biochem J. 1964 Jul;92(1):184-205. doi: 10.1042/bj0920184.
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A study of properties of renal microbodies of the rat.大鼠肾脏微体性质的研究。
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Ultrastructural localization of D-amino acid oxidase in microperoxisomes of the rat nervous system.大鼠神经系统微过氧化物酶体中D-氨基酸氧化酶的超微结构定位
J Histochem Cytochem. 1979 Mar;27(3):735-45. doi: 10.1177/27.3.39097.

引用本文的文献

1
In situ heterogeneity of peroxisomal oxidase activities: an update.过氧化物酶体氧化酶活性的原位异质性:最新进展。
Histochem J. 1996 Jun;28(6):401-29. doi: 10.1007/BF02331433.
2
Quantitative comparison between the gel-film and polyvinyl alcohol methods for dehydrogenase histochemistry reveals different intercellular distribution patterns of glucose-6-phosphate and lactate dehydrogenases in mouse liver.凝胶薄膜法与聚乙烯醇法用于脱氢酶组织化学的定量比较揭示了小鼠肝脏中葡萄糖-6-磷酸脱氢酶和乳酸脱氢酶不同的细胞间分布模式。
Histochem J. 1994 Jun;26(6):480-6. doi: 10.1007/BF00157893.
3
Distribution of peroxisomes (microbodies) in the nephron of the rat: a cytochemical study.
大鼠肾单位中过氧化物酶体(微体)的分布:细胞化学研究
J Cell Biol. 1969 Aug;42(2):501-18. doi: 10.1083/jcb.42.2.501.
4
Cytochemical localization by ferricyanide reduction of -hydroxy acid oxidase activity in peroxisomes of rat kidney.用铁氰化物还原法对大鼠肾脏过氧化物酶体中α-羟酸氧化酶活性进行细胞化学定位。
Histochemie. 1971;27(2):137-58. doi: 10.1007/BF00284956.
5
Ultrastructural observations on the pars descendens of the proximal tubule in the kidney of the male rat.雄性大鼠肾脏近端小管降部的超微结构观察
Z Zellforsch Mikrosk Anat. 1973 Feb 6;136(4):479-99. doi: 10.1007/BF00307365.
6
The occurrence in yeast of cytoplasmic granules which resemble microbodies.酵母中出现类似于微体的细胞质颗粒。
J Cell Biol. 1968 May;37(2):555-9. doi: 10.1083/jcb.37.2.555.
7
The histochemical localization of lactic dehydrogenase isoenzymes in the rat nephron by means of an improved polyvinyl alcohol method.用改良的聚乙烯醇法对大鼠肾单位中乳酸脱氢酶同工酶进行组织化学定位。
Histochemie. 1969;20(3):250-65. doi: 10.1007/BF00306013.
8
A zonal rotor method for the preparation of microperoxisomes from epithelial cells of guinea pig small intestine.一种从豚鼠小肠上皮细胞制备微型过氧化物酶体的区带转子法。
J Cell Biol. 1974 Apr;61(1):123-33. doi: 10.1083/jcb.61.1.123.
9
Electron microscopic cytochemical localization of alpha-hydroxyacid oxidase in rat kidney cortex. Heterogeneous staining of peroxisomes.大鼠肾皮质中α-羟酸氧化酶的电子显微镜细胞化学定位。过氧化物酶体的异质性染色。
Histochemistry. 1986;85(5):411-8. doi: 10.1007/BF00982671.
10
Peroxisomes in wild-type and rosy mutant Drosophila melanogaster.野生型和玫瑰色突变型黑腹果蝇中的过氧化物酶体。
Proc Natl Acad Sci U S A. 1987 Nov;84(21):7433-7. doi: 10.1073/pnas.84.21.7433.