A correlation between soluble brain nitric oxide synthase and NADPH-diaphorase activity is only seen after exposure of the tissue to fixative.

作者: Takahiro Matsumoto , Masaki Nakane , Jennifer S. Pollock , Jane E. Kuk , Ulrich Förstermann

DOI: 10.1016/0304-3940(93)90673-9

关键词:

摘要: Abstract In histochemical studies using fixed brain tissue, NADPH-diaphorase has been found to be colocalized with soluble nitric oxide synthase. the present study, fresh tissues from eight different regions of rat brain, activity was mostly in particulate fraction, whereas most synthase located cytosolic fraction. Also, distribution among that Pretreatment fractions paraformaldehyde virtually abolished 40–60% remained intact These results suggest during fixation is inactivated and only some associated remains intact.

参考文章(15)
Harald H. H. W. Schmidt, R. M. Smith, M. Nakane, Ferid Murad, Ca2+/calmodulin-dependent NO synthase type I: a biopteroflavoprotein with Ca2+/calmodulin-independent diaphorase and reductase activities. Biochemistry. ,vol. 31, pp. 3243- 3249 ,(1992) , 10.1021/BI00127A028
M.C. Kemp, D.R. Kuonen, A. Sutton, P.J. Roberts, Rat brain NADPH-dependent diaphorase. A possible relationship to cytochrome P450 reductase. Biochemical Pharmacology. ,vol. 37, pp. 3063- 3070 ,(1988) , 10.1016/0006-2952(88)90302-4
Kazuaki Hiki, Ryuichi Hattori, Chuichi Kawai, Yoshiki Yui, Purification of insoluble nitric oxide synthase from rat cerebellum. Journal of Biochemistry. ,vol. 111, pp. 556- 558 ,(1992) , 10.1093/OXFORDJOURNALS.JBCHEM.A123795
N.J. Dun, S.L. Dun, U. Forstermann, L.F. Tseng, Nitric oxide synthase immunoreactivity in rat spinal cord Neuroscience Letters. ,vol. 147, pp. 217- 220 ,(1992) , 10.1016/0304-3940(92)90599-3
H. H. Schmidt, J. S. Pollock, M. Nakane, L. D. Gorsky, U. Forstermann, F. Murad, Purification of a soluble isoform of guanylyl cyclase-activating-factor synthase. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 88, pp. 365- 369 ,(1991) , 10.1073/PNAS.88.2.365
T. M. Dawson, D. S. Bredt, M. Fotuhi, P. M. Hwang, S. H. Snyder, Nitric oxide synthase and neuronal NADPH diaphorase are identical in brain and peripheral tissues. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 88, pp. 7797- 7801 ,(1991) , 10.1073/PNAS.88.17.7797
D. S. Bredt, S. H. Snyder, Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 87, pp. 682- 685 ,(1990) , 10.1073/PNAS.87.2.682
David S. Bredt, Charles E. Glatt, Paul M. Hwang, Majid Fotuhi, Ted M. Dawson, Solomon H. Snyder, Nitric oxide synthase protein and mRNA are discretely localized in neuronal populations of the mammalian CNS together with NADPH diaphorase Neuron. ,vol. 7, pp. 615- 624 ,(1991) , 10.1016/0896-6273(91)90374-9
Takahiro Matsumoto, Jennifer S. Pollock, Masaki Nakane, Ulrich Förstermann, Developmental changes of cytosolic and particulate nitric oxide synthase in rat brain. Developmental Brain Research. ,vol. 73, pp. 199- 203 ,(1993) , 10.1016/0165-3806(93)90139-2
Ulrich Förstermann, Lee D. Gorsky, Jennifer S. Pollock, Harald H.H.W. Schmidt, Michael Heller, Ferid Murad, Regional distribution of EDRF/NO-synthesizing enzyme(s) in rat brain. Biochemical and Biophysical Research Communications. ,vol. 168, pp. 727- 732 ,(1990) , 10.1016/0006-291X(90)92382-A