Keizer I, Roggenkamp R, Harder W, Veenhuis M
Laboratory for Electron Microscopy, Biological Centre, University of Groningen, Haren, Netherlands.
FEMS Microbiol Lett. 1992 May 15;72(1):7-11. doi: 10.1016/0378-1097(92)90481-3.
We have studied the intraperoxisomal location of catalase in peroxisomes of methanol-grown Hansenula polymorpha by (immuno)cytochemical means. In completely crystalline peroxisomes, in which the crystalline matrix is composed of octameric alcohol oxidase (AO) molecules, most of the catalase protein is located in a narrow zone between the crystalloid and the peroxisomal membrane. In non-crystalline organelles the enzyme was present throughout the peroxisomal matrix. Other peroxisomal matrix enzymes studied for comparison, namely dihydroxyacetone synthase, amine oxidase and malate synthase, all were present throughout the AO crystalloid. The advantage of location of catalase at the edges of the AO crystalloids for growth of the organism on methanol is discussed.
我们通过（免疫）细胞化学方法研究了甲醇培养的多形汉逊酵母过氧化物酶体中过氧化氢酶在过氧化物酶体内的定位。在完全结晶的过氧化物酶体中，其结晶基质由八聚体醇氧化酶（AO）分子组成，大部分过氧化氢酶蛋白位于类晶体和过氧化物酶体膜之间的狭窄区域。在非结晶细胞器中，该酶存在于整个过氧化物酶体基质中。为作比较而研究的其他过氧化物酶体基质酶，即二羟基丙酮合酶、胺氧化酶和苹果酸合酶，均存在于整个AO类晶体中。文中讨论了过氧化氢酶定位于AO类晶体边缘对该生物体在甲醇上生长的优势。
