Showing papers by "Peter Klatt published in 1994"
TL;DR: The data indicate that brain NO synthase exhibits a highly specific binding site for (6R)-5,6,7,8-tetrahydro-L-biopterin, which allosterically interacts with the substrate domain and may be located proximal to the prosthetic heme group of NO synth enzyme.
215 citations
TL;DR: After prolonged incubation periods, NG-nitro-L-arginine induced a rapid inactivation of the enzyme, whereas the methyl derivative turned out to be a substrate of NO synthase, which was slowly converted into stoichiometric amounts of NO and L-citrulline.
163 citations
TL;DR: 7-Nitro-indazole resembled imidazole, a known heme-site inhibitor of NOS, and was a purely competitive inhibitor of L-citrulline formation and blocked H2O2 formation at similar concentrations.
129 citations
TL;DR: It is shown that peroxynitrite induces spectral changes of oxyhaemoglobin identical with those elicited by NO, demonstrating that electrochemical detection has an advantage over the oxyhaenoglobin method for specific determination of NO.
Abstract: A frequently applied photometrical assay of NO is based on the reaction of NO with oxyhaemoglobin. This study shows that peroxynitrite induces spectral changes of oxyhaemoglobin identical with those elicited by NO. Like a variety of other agents, peroxynitrite did not interfere with NO measurements using a Clark-type electrode, demonstrating that electrochemical detection has an advantage over the oxyhaemoglobin method for specific determination of NO.
68 citations
TL;DR: Rat brain nitric oxide synthase was expressed to a high level in baculovirus-infected insect cells and purified to apparent homogeneity by affinity chromatography.
Abstract: Rat brain nitric oxide synthase was expressed to a high level in baculovirus-infected insect cells and purified to apparent homogeneity by affinity chromatography. The enzyme had a specific activity of approximately 1 mumol of citrulline.min-1.mg of protein-1 and contained 0.93, 0.45, 0.18 and 0.23 mol of haem, (6R)-5,6,7,8-tetrahydro-L-biopterin (H4biopterin), FAD and FMN per mol of subunit respectively.
53 citations
TL;DR: Characterization of the transport sites revealed that uptake of L-NMA is mediated by a cationic amino acid transporter (system y+) whereas a neutral amino acids transporter ( system L) accounts for the uptake ofL-NNA.
Abstract: Uptake of the nitric oxide synthase inhibitors NG-methyl-L-arginine (L-NMA) and NG-nitro-L-arginine (L-NNA) by macrophages is mediated by two different mechanisms. Activation of the cells with cytokines resulted in an up-regulation of L-NMA uptake but did not affect L-NNA transport. Characterization of the transport sites revealed that uptake of L-NMA is mediated by a cationic amino acid transporter (system y+) whereas a neutral amino acid transporter (system L) accounts for the uptake of L-NNA.
43 citations
TL;DR: It is demonstrated that imidazole exerts its effects on NOS in an l‐arginine‐competitive manner and that the substrate site of the enzyme may be identical with the prosthetic heme group.
28 citations