Copper enzymes in isolated chloroplasts. polyphenoloxidase in beta vulgaris
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TLDR
Evidence that a copper enzyme, polyphenoloxidase (otherwise known as tyrosinase or catecholase), is localized in the chloroplasts of spinach beet (chard), Beta vu?garis is presented.Abstract:
The chloroplast, as the seat of chlorophyll pigments in plants, occupies a unique position in the economy of the green cell. In recent years there has been a renewed interest in the reactions and properties of chloroplasts as a result of the work of Hill (11, 12) and Hill and Scarisbrick (13, 14) who demonstrated that the reaction characteristic of photosynthesis in green plants, the evolution of oxygen, occurs in appreciable quantities in isolated chloroplasts under the influence of light and in the presence of suitable oxidants (2, 7, 8, 26). In the course of an investigation of oxygen evolution by isolated chloroplasts it was deemed important to explore their enzymatic composition. Of special interest were considered enzymes capable of participating in oxidation-reduction reactions, and more particularly, those localized principally, if not entirely, in the chloroplasts. This paper presents evidence that a copper enzyme, polyphenoloxidase (otherwise known as tyrosinase or catecholase), is localized in the chloroplasts of spinach beet (chard), Beta vu?garis.read more
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References
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TL;DR: This paper deals with the estimation of chlorophyll in plant extracts by application of absorption coefficients of the isolated solid chlorophylla components, and the question of artifacts is automatically clarified.
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Oxygen Evolved by Isolated Chloroplasts
TL;DR: The hæmoglobin method, originally used by Hoppe-Seyler to demonstrate oxygen from green plants, has been applied to study the oxygen evolution of isolated chloroplasts exposed to light.
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Oxygen Produced by Isolated Chloroplasts
TL;DR: Inman (1935) brought further evidence as to the enzymic nature of the process, and showed also that fresh green extracts of many phanerogams will evolve oxygen in light, using the bacterial mathod.