Nitric oxide synthase activity.
Nitric oxide synthase activity.
复制标题
一氧化氮合酶活性。
DOI:
--
复制
发表时间:
1996
影响因子:
3.2
通讯作者:
W. Frederiks
中科院分区:
文献类型:
--
作者:
W. Frederiks
With great interest I have read the paper of Mehdizadeh et al. (19951) in the Journal of Histochemirtry and Cytochemishy on “Measurement of nitric oxide synthase activity in sections of rat liver.’’ Until now, in situ localization of NOS was performed with immunohistochemical techniques, which detect the protein, or in situ hybridization, which demonstrates the “A. The NADPH diaphorase method has been claimed to demonstrate NOS activity, but this procedure is not appropriate to detect the enzyme activity under all conditions (Beesley, 1995). Therefore, it is very useful to develop in situ techniques for the demonstration of NOS activity. The principle introduced by Mehdizadeh et al. (1995a) is based on the capacity of nitric oxide to stimulate guanylate cyclase activity. This is an original idea, and may give rise to a valid procedure to detect NOS activity when both enzymes are present in the same cell and when a valid method is available to demonstrate soluble guanylate cyclase activity. The last prerequisite has been fulfilled by Mehdizadeh et al. (1995b). However, with respect to the localization of the two related enzymes, Mehdizadeh et al. (1995a) assume that NOS activity is present in Kupffer cells and that soluble guanylate is present in hepatocytes. As a consequence, diffusion of nitric oxide from Kupffer cells to hepatocytes should occur. According to Mehdizadeh et al. (1995a). this diffusion can be facilitated by decreasing the concentration of the stabilizer in the incubation medium from 35% to 30%. However, this means that the proposed histochemical approach does not provide any information on the precise in situ localization of NOS activity, which is the characteristic of histochemistry. The method may give indications for the total NOS activity in rat liver if diffusion of nitric oxide is not limited. However, for that purpose well-established biochemical methods are available using tissue or cell homogenates, cell fractions, and subcellular fractions (Curran et al., 1989). Vol. 44, No. 11, p. 1341. 1996 Printd in USA.