𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Activities of arginase, transamidinase, and ornithine aminotransferase in glia, neurons, and synaptosomes

✍ Scribed by M. Swamy; K. P. Shrivastaw; M. S. K. Prasad; Professor B. Sadasivudu


Publisher
John Wiley and Sons
Year
1983
Tongue
English
Weight
356 KB
Volume
10
Category
Article
ISSN
0360-4012

No coin nor oath required. For personal study only.

✦ Synopsis


The regional, cellular, and subcellular distribution of some enzymes of the urea cycle in brain is not clearly known. Glja, neurons, and synaptosomes have been prepared from rat cerebral cortex and arginase (EC 3.5.3. I ) , transamidinase (EC 2.1.4.1), and ornithine aminotransferase (EC 2.6.1.13) have been estimated in order to understand the metabolic and functional role of these enzymes. It has been observed that arginasc is predominantly localized in synaptosomes and neurons. The ornithine aminotransferase was found to be high in glial cells and very high in synaptosomes (higher than arginase). Transamidinase was mostly localized in glial cells. The implication of these results has been discussed in relation to a possible role of ornithine acting as a precursor of glutamate in glutametargic nerve endings and its possible participation in the glutamate-glutamine cycle.


📜 SIMILAR VOLUMES


Identification of reciprocally regulated
✍ Adrian A. Cameron; Gordon Vansant; Wen Wu; Dennis J. Carlo; Charles R. ILL 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 301 KB

## Abstract Differential gene expression in the rat after injury of dorsal root ganglion neurons in vivo, and simulation injury of Schwann cells and oligodendrocytes in vitro was analyzed using high‐density cDNA microarrays. The analyses were carried out to study the genetic basis of peripheral ner

Differential regulation of BACE1 promote
✍ Krystyn Z. Bourne; Diana C. Ferrari; Christine Lange-Dohna; Steffen Roßner; Thom 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 484 KB

## Abstract The brains of Alzheimer's disease (AD) patients display cerebrovascular and parenchymal deposits of β‐amyloid (Aβ) peptides, which are derived by proteolytic processing by the β‐site APP‐cleaving enzyme 1 (BACE1) of the amyloid precursor protein (APP). The rat BACE1 promoter has a nucle