[Quantitative spectral determination of manganese, nickel, copper, chromium, iron, barium, strontium, vanadium and lead in blood with a quantometer].
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Barium↗
Biomedical subjects
A V Kariakin
Publications and source records attributed to A V Kariakin.
[Initial processes of the interaction between chlorophyll and methylviologen].
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Ascorbic Acid↗
[Intermediate states in photoreduction of chlorophyll].
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Ascorbic Acid↗
[Spectrum and photochemical properties of chlorophyll interacting with albumin].
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Chlorophyll↗
[Study of primary photochemical interactions of chlorophyll pigments with electron acceptors and donors by use of impulse spectroscopy].
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Chemical Phenomena↗
[Concentration of several polyvalent metals in blue-green algae].
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Biological Evolution↗
[Electron transfer between microsomal and mitochondrial membranes].
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Aniline Compounds↗
[Water state in substances participating in photosynthesis].
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Adenine Nucleotides↗
[Infrared spectra of aqueous solutions of certain amino acids].
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Amino Acids↗
[Infrared spectra and amphoteric structure of amino acids].
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Amino Acids↗
[Triplet-triplet energy transport and photooxidation of chlorophyll].
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Chlorophyll↗
[Infrared absorption spectral study of the reaction of protein with dyes and chlorophyllin].
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Acridines↗
[Study of the interaction of chlorophyll (a + b) with glycinin at various pH values].
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Buffers↗
[Use of a laser atomizer for the atomic absorption determination of the thallium content of bones].
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Autopsy↗
[Absorption spectra and magnetic circular dichroism of ferrocytochrome b5 formed during low temperature reduction in a nonequilibrium state].
Under gamma-irradiation of frozen water--glycerol solutions of ferrocytochrome b5 at 77 degrees K ferrocytochrome b5 in a non-equilibrium state is formed. Its absorption and MCD spectra are displaced by 1,5 nm to the long wave region. When the temperature is increased to 140 degrees K the non-equilibrium form of reduced protein is relaxes. A comparison of optical characteristics of ferrocytochrome b5 in equilibrium and non-equilibrium states shows that the structure of the protein active centre slightly depends on the state of metal oxidation. It is concluded on the basis of earlier published data on low temperature reduction of different electron transport proteins that a small effect of the oxidation state of a metal ion on the active centre structure is a common property of all the electron transport proteins. This phenomenon makes these systems an effective carrier of electrons.
Animals↗