نتایج جستجو برای: c light

تعداد نتایج: 1415809  

Journal: :Proceedings of the National Academy of Sciences 1978

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1981
J O Alben P P Moh F G Fiamingo R A Altschuld

Carbon monoxide bound to iron or copper in substrate-reduced mitochondrial cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) from beef heart has been used to explore the structural interaction of the a3 heme-copper pocket at 15 K and 80 K in the dark and in the presence of visible light. The vibrational absorptions of CO measured by a Fourier transform infrared interfer...

Journal: :Advanced photonics research 2022

Up-Conversion Luminescence Feng Liu, Jiahua Zhang and co-workers explore an innovative way of using visible light for disinfection application by introducing a transmissive remote phosphor-converted source phosphor composite film, which gives ultraviolet-C emission upon excitation with blue lasers. More information can be found in article number 2200106.

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 2000
A Wenzel C Grimm A Marti N Kueng-Hitz F Hafezi G Niemeyer C E Remé

White light (5 klux for 2 hr) induces apoptosis of rod photoreceptors in wild-type mice (c-fos(+/+)) within 24 hr, whereas rods of c-fos knock-out mice (c-fos(-/-)) are protected (). The range of this protection was tested by analyzing retinas of c-fos(+/+) and c-fos(-/-) mice up to 10 d after exposure to threefold increased light intensities (15 klux for 2 hr). In c-fos(-/-) mice, rods were un...

A major problem in the formulation of therapeutic proteins is the irreversible protein aggregation. Recombinant human interferon alpha2b (rhIFN2b) has poor stability and undergoes physical degradation. The aim of this study was to investigate the effect of solution conditions on the heat-induced aggregation of rhIFNα2b. The protein was incubated for 1 h at 40°C–70°C and for up to 240 h at 50C...

A major problem in the formulation of therapeutic proteins is the irreversible protein aggregation. Recombinant human interferon alpha2b (rhIFN2b) has poor stability and undergoes physical degradation. The aim of this study was to investigate the effect of solution conditions on the heat-induced aggregation of rhIFNα2b. The protein was incubated for 1 h at 40°C–70°C and for up to 240 h at 50C...

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