Bondy S C
Neurochem Res. 1986 Dec;11(12):1653-62. doi: 10.1007/BF00967743.
The enzymic decarboxylation of ornithine by adult rat brain largely occurs in the particulate fraction. The activity is primarily due to ornithine decarboxylase (ODC) as evidenced by several criteria: the concurrent production of equimolar amounts of CO2 and putrescine, the sensitivity of the reaction to difluoromethylornithine (DFMO), a specific inhibitor of ODC, the lack of major effect of two inhibitors of ornithine-2-oxo-acid transaminase, upon the DFMO-sensitive component of decarboxylation, the failure to profoundly reduce decarboxylation activity in the presence of a large excess of many aminoacids which could compete for non-specific decarboxylases. The insoluble ODC activity appears largely within synaptosomal and mitochondrial-enriched morphological fractions, yet cannot be attributed to trapped soluble ODC. Particulate ODC has a pH optimum and kinetic parameters that differ from those of soluble cerebral ODC.
成年大鼠脑内鸟氨酸的酶促脱羧反应主要发生在微粒部分。该活性主要归因于鸟氨酸脱羧酶(ODC),这可通过以下几个标准来证明:同时产生等摩尔量的二氧化碳和腐胺,反应对ODC的特异性抑制剂二氟甲基鸟氨酸(DFMO)敏感,两种鸟氨酸-2-氧代酸转氨酶抑制剂对脱羧反应中DFMO敏感成分无主要影响,在存在大量可竞争非特异性脱羧酶的多种氨基酸的情况下,脱羧活性未能显著降低。不溶性ODC活性主要出现在富含突触体和线粒体的形态学部分,但不能归因于截留的可溶性ODC。微粒体ODC的最适pH值和动力学参数与可溶性脑ODC不同。