| Literature DB >> 7689718 |
T Matsumoto1, M Nakane, J S Pollock, J E Kuk, U Förstermann.
Abstract
In histochemical studies using fixed brain tissue, NADPH-diaphorase has been found to be colocalized with soluble nitric oxide synthase. In the present study, using fresh tissues from eight different regions of rat brain, NADPH-diaphorase activity was found mostly in the particulate fraction, whereas most of the nitric oxide synthase activity was located to the cytosolic fraction. Also, the distribution of NADPH-diaphorase activity among brain regions was different from that of nitric oxide synthase. Pretreatment of the fractions with paraformaldehyde virtually abolished the NADPH-diaphorase activity in the particulate fraction, whereas 40-60% of the NADPH-diaphorase activity remained intact in the cytosolic fraction. These results suggest that during fixation most NADPH-diaphorase activity is inactivated and only some of the NADPH-diaphorase activity associated with soluble nitric oxide synthase remains intact.Entities:
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Year: 1993 PMID: 7689718 DOI: 10.1016/0304-3940(93)90673-9
Source DB: PubMed Journal: Neurosci Lett ISSN: 0304-3940 Impact factor: 3.046