Topic
Substrate (chemistry)
About: Substrate (chemistry) is a research topic. Over the lifetime, 35902 publications have been published within this topic receiving 740722 citations. The topic is also known as: enzyme substrate.
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TL;DR: In this paper, a new colloidal processing method for near net shaping ceramic components is outlined, which relies on electrostatic stabilized ceramic suspensions and it’s destabilization by time delayed in situ reactions.
188 citations
TL;DR: Comparison of the substrate specificity for these systems (kcat/KD) indicates a 5- and 7-fold decrease in specificity for the mutant enzyme and thiocamphor-wild type complex, respectively.
188 citations
TL;DR: In this paper, the authors described a tape-type magnetic recording media (I) including a non-magnetic substrate (III), at least one film applied to the substrate and an inorganic acicular pigment suitable for use as a supporting pigment, the ratio of the mean length to the mean diameter of the pigment (II) being at least 3 and the mean modulus of elasticity of the films being not less than 15 GPa in the longitudinal direction of the magnetic medium.
Abstract: Described are tape-type magnetic recording media (I) including a non-magnetic substrate (III), at least one film applied to the substrate and, in at least one of these films, an inorganic acicular pigment (II) suitable for use as a supporting pigment, the ratio of the mean length to the mean diameter of the pigment (II) being at least 3 and the mean modulus of elasticity of the films being not less than 15 GPa in the longitudinal direction of the tape-type recording medium (I).
187 citations
TL;DR: A new one-step method for the light and electron microscopic localization of the ouabain-sensitive, K-dependent p-nitrophenylphosphatase (K-NPPase) activity of the Na-K-ATPase complex is introduced.
Abstract: A new one-step method for the light and electron microscopic localization of the ouabain-sensitive, K-dependent p-nitrophenylphosphatase (K-NPPase) activity of the Na-K-ATPase complex is introduced. The incubation medium contains p-nitrophenylphosphate (NPP) as substrate, lead citrate as the capture reagent, and dimethylsulfoxide (DMSO) as an activator. It is usable at the optimal pH of the K-NPPase, which is about pH 9.0 in the presence of 25% of DMSO. The effects of fixation, lead concentration, and DMSO on the enzyme activity were studied using rat kidney as a test tissue. The fixation of tissues in a mixture of 2% paraformaldehyde and 0.5% glutaraldehyde for 60 min at 0 degrees--4 degrees C preserved 45% of the enzyme activity. In the absence of DMSO, lead citrate (4.0 mM) caused 82% inhibition of the enzyme activity in fixed tissue. However, the addition of DMSO (25%) caused about 3-fold activation of the remaining activity. Cytochemical demonstration of the ouabain-sensitive K-NPPase activity was successfully made by this method at both light and electron microscopic levels.
187 citations
187 citations