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- W2187008630 abstract "Thesubstructural organization ofcompletely crystalline peroxisomes present inHansenula polymorpha cells grownunder methanol limitation inachemostat wasinvestigated bydifferent cytochemical andultrastructural techniques. Timedependent cytochemical staining experiments indicated thatactivities ofthetwo mainconstituents ofthese organelles, namely, alcohol oxidase andcatalase, were present throughout thecrystalline matrix. Catalase wascompletely removed from isolated peroxisomes byosmotic shocktreatment. After suchtreatment, the ultrastructure ofthecrystalline matrix oftheorganelles remained virtually intact. Because alcohol oxidase activity wasstill present inthis matrix, itwasconcluded thatalcohol oxidase protein istheonlystructural element oftheperoxisomal crystalloids. Themolecular architecture ofthecrystalloids wasinvestigated in ultrathin cryosections whichpermitted recognition ofindividual molecules inthe crystalline matrix. Depending ontheplane ofsectioning, different crystalline patterns wereobserved. Tilting experiments indicated thatthese images were caused bysuperposition ofoctameric alcohol oxidase molecules arranged ina tetragonal lattice. Athree-dimensional modelofthecrystalloid ispresented. The" @default.
- W2187008630 created "2016-06-24" @default.
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- W2187008630 date "1981-01-01" @default.
- W2187008630 modified "2023-09-27" @default.
- W2187008630 title "Substructure ofCrystalline Peroxisomes inMethanol-Grown Hansenula polymorpha: Evidence foranInVivoCrystal of" @default.
- W2187008630 hasPublicationYear "1981" @default.
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