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L-α-羟酸氧化酶在猴肾哑铃形过氧化物酶体致密棒中的免疫细胞化学定位。

Immunocytochemical localization of L-alpha-hydroxyacid oxidase in dense bar of dumb-bell-shaped peroxisomes of monkey kidney.

作者信息

Yokota S, Hashimoto T

机构信息

Department of Anatomy, Yamanashi Medical School, Japan.

出版信息

Histochem Cell Biol. 1995 Jul;104(1):55-61. doi: 10.1007/BF01464786.

Abstract

Localization of the B of L-alpha hydroxyacid oxidase (HOX-B) in monkey kidney peroxisomes was investigated by immunoelectron microscopic techniques. Kidneys of Japanese monkeys, Macaca fuscata, were fixed with 4% paraformaldehyde + 0.25% glutaraldehyde and embedded in LR White resin. Thin sections were stained for HOX-B and catalase by the immunogold technique. HOX-B was localized in the marginal plates of normal peroxisomes and the dense bar of dumb-bell-shaped peroxisomes. Catalase was detected in the matrix of normal peroxisomes and in the terminal dilatations of dumb-bell-shaped peroxisomes. There were no gold particles indicating presence of catalase associated with the marginal plates or with the dense bars. Immunoblot analysis of monkey kidney homogenate showed that HOX-B has a molecular mass of 42 kDa that was slightly larger than that of rat kidney HOX-B (39 kDa). The results show that the dense bar of dumb-bell-shaped peroxisomes in monkey kidney is composed of at least HOX-B and is a variation of the marginal plates.

摘要

通过免疫电子显微镜技术研究了L-α羟酸氧化酶(HOX-B)在猴肾过氧化物酶体中的定位。用4%多聚甲醛+0.25%戊二醛固定日本猕猴(Macaca fuscata)的肾脏,并包埋于LR White树脂中。用免疫金技术对超薄切片进行HOX-B和过氧化氢酶染色。HOX-B定位于正常过氧化物酶体的边缘板和哑铃形过氧化物酶体的致密条带中。在正常过氧化物酶体的基质和哑铃形过氧化物酶体的末端扩张中检测到过氧化氢酶。没有金颗粒表明过氧化氢酶存在于边缘板或致密条带中。猴肾匀浆的免疫印迹分析表明,HOX-B的分子量为42 kDa,略大于大鼠肾HOX-B(39 kDa)。结果表明,猴肾中哑铃形过氧化物酶体的致密条带至少由HOX-B组成,是边缘板的一种变体。

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