Über die Wirkung des blauen und roten Spektralbereichs auf die Zusammensetzung und Zellteilung synchronisierter Chlorellen

Kowallik, Wolfgang

doi:10.1007/bf01949671

Cited by 81 publications

(20 citation statements)

References 30 publications

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“…Whereas the formation of RNA proceeds almost in parallel with that of protein, the formation of DNA takes place only slowly during the growing phase and occurs abruptly at a considerable rate at the stages of ripening (L2---> L4). Such a sudden increase of DNA occurring at a cer tain stage of ripening was later reported for C. pyrenoidosa (34,82,94,100,138,141,143,144,158,193,195,214); the high temperature Chlorella (57); and E. gracilis, strain Z (32) [but not for another strain of E. gracilis (19) and ChI. moewusii (12)].…”

Section: Biochemical Events Occurring In Normal Cell Cyclesmentioning

confidence: 70%

“…It was found that the ratio of carbohydrate to protein in algal cells was higher with red light and lower with blue light as compared with the value obtained with white light. In the red-light experiment, carbohydrate synthesis predominated at the beginning of the light period and was grad ually followed by protein synthesis (82). A converse relation was observed in the blue-light experiment.…”

Section: L\-10rphological and Physiological Events Occurring In Normmentioning

confidence: 76%

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Synchronous Cultures of Algae

Tamiya¹

1966

Annu. Rev. Plant. Physiol.

121

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Section: Biochemical Events Occurring In Normal Cell Cyclesmentioning

confidence: 70%

Section: L\-10rphological and Physiological Events Occurring In Normmentioning

confidence: 76%

Synchronous Cultures of Algae

Tamiya¹

1966

Annu. Rev. Plant. Physiol.

121

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“…211-1lh/20 of the Culture Collection of Algae, (Professor E. G. Pringsheim), Institute of Plant Physiology, University of Gottingen, Germany. This organism was grown in glass tubes 25 cm long and 3.5 cm wide containing a sterile mineral medium suitable for autotroph(ic growth of unicellullar green algae (6) After the cell suspensioni had been saturated with air and pipetted into the vessel (1), the latter was closed tight without leaving a bubble. The oxygen consumption was recorded during the first 30 minutes in the dark, then for 40 minutes longer in the light.…”

Section: Methodsmentioning

confidence: 99%

Action Spectrum for an Enhancement of Endogenous Respiration by Light in Chlorella

Kowallik

1967

Plant Physiol.

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Sumntmary. The oxygen consumption of a starved chlorophyll-free, yellow mutant of Chlorella vulgaris is enihanced by very smalq amounts of blue light (X 450 mu); a saturation level is reached at about 500 ergs cm 2 sec'l. At that intensity the respiration is about 3 times greater than in the dark. An action spectru-m for the enhancement of respiration shows 2 peaks around X 450 and 375 mju. Fliavins and cis-caroteno'ids are dis;cussed as the pigments involved.Fifteen years ago Voskresenskaja (13) reported that leaves of higher plants contain more protein after growth in blue ligh't thian after growth in red light and since then this restlt has been confirmed several times (1,2,5,9). I't was also exten(led to several green algae (6,11).WVhile looking for the primary photochemistry in this process we found recently that blue light enhanced the endogenous respiration of starved Chlorella markedly in a reversible manner (7,8).The first step in the search for the photochemically active pigment was to exclude chlorophyll by demonstrating the same effect in a chlorophyll-free, yellow mutant of Chlorella. Lacking an overlapp:ng chlorophyll absorption in the blue, this yellow organism was obviously the very object for measuring an action spectrum of the enhancement o,f respiration by light. The result we have obtained points to participation of either a cis-carotenoid or a flavin. Materials and MethodsThe The oxygen sensor is inserted in one wall of a 2X2X2 cm plexiglass vessel which can be closecl air tight. Figure 1 illustrates the set ulp. The vessel with the sensor and the suspension (1) sits in a bigger plexiglass vessel (k) which serves as a water bath. The latter is connected to a thermostat and portable cooling bath. The vessel is placed on top of a magnetic stirrer (i) w-hich turns at 1000 rpm. Before closing the vessel (1) its contents can be equilibrated with a gas stream brought uip to temperature by passing it through

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“…Euglena gracilis Z. Klebs was cultured phototrophically with air (3) on the inorganic medium of Cramer and Myers (2). The yellow mutant Chlorella vulgaris 211-11 h/20 was grown as reported previously (14), on a glucose medium (13).…”

mentioning

confidence: 99%

Serological Characterization of the Glycolate-oxidizing Enzymes from Tobacco, Euglena gracilis, and a Yellow Mutant of Chlorella vulgaris

Codd

Schmid

1972

Plant Physiol.

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An antiserum to tobacco glycolate oxidase has been prepared by injection of the purified enzyme into rabbits. Double gel diffusion tests between the antiserum and purified antigen and also with a crude tobacco preparation gave a single immunoprecipitation band. (1,26,27,29). Artificial dyes such as DCPIP1 and methylene blue can function as electron acceptors in the reaction (3,8), and the enzyme may, under certain conditions, donate electrons to quinones (5,11,12).Glycolate-oxidizing enzymes have also been detected in several unicellular green algae (3, 15,19,28). The enzyme prepared from Euglena gracilis Z. Klebs, Chlorella pyrenoidosa 211/8p, and Chiamydomonas reinhardtii Danglard (-) 90, all from the Cambridge Culture Collection, functions with DCPIP as electron acceptor but does not link to oxygen (3). Similar results were obtained with enzyme preparations from E. gracilis and Chlamydomonas reinhardtii (-) 90 from the Indiana Algal Culture Collection and with Acetabularia mediterranea (19,20). Furthermore, a glycolate-oxidizing enzyme with no 02 requirement has been found in the blue-green algae Anabaena flos-aquae and an Oscillatoria species (9). No requirement for FMN was observed in the green algal and A. flos-aquae preparations, although a slight enhancement by FMN was noted with the Oscillatoria extract (3,9,20,28). This enzyme found in the above algae is referred to in the 'Abbreviations: DCPIP: 2,6-dichlorophenolindophenol; DEAE: diethylaminoethyl.literature as glycolate dehydrogenase. Neither the higher plant nor the algal enzymes described show an absolute specificity for glycolate. The former can also oxidize L-lactate but not the D-isomer (1). The algal enzymes readily use D-lactate as a substrate but only slowly attack the L-form (10,20).An algal glycolate-oxidizing enzyme showing a mixture of the criteria described has been characterized. Intact cells and enzyme preparations from green Chlorella vulgaris 211-llh (Algal Culture Collection, Gottingen) and the chlorophyllfree mutant Chlorella vulgaris 211-1 lh/20 (25) show a glycolate-dependent oxygen consumption, similar to that of higher plants (14). However, the addition of FMN does not affect enzyme activity in vitro, and both the n-and L-lactate isomers are oxidized, at approximately equal rates (6,14).The present investigation was carried out to characterize further plant glycolate-oxidizing enzymes from a serological approach, using an antiserum to the pure tobacco enzyme. Effects of this antibody to glycolate oxidase on immunoprecipitation and inhibition of the homologous enzyme are reported. The antibody has also been tested against enzyme preparations from E. gracilis, taken as an example of the algal glycolate dehydrogenase and against Chlorella vulgaris 211-1lh/20, which exhibits glycolate oxidase activity.MATERIALS AND METHODS Plant Material. Nicotiana tabacum L. cv. John Williams' Broadleaf was grown as described previously (23). Euglena gracilis Z. Klebs was cultured phototrophically with air (3) on the inorganic medium of C...

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Über die Wirkung des blauen und roten Spektralbereichs auf die Zusammensetzung und Zellteilung synchronisierter Chlorellen

Cited by 81 publications

References 30 publications

Synchronous Cultures of Algae

Synchronous Cultures of Algae

Action Spectrum for an Enhancement of Endogenous Respiration by Light in Chlorella

Serological Characterization of the Glycolate-oxidizing Enzymes from Tobacco, Euglena gracilis, and a Yellow Mutant of Chlorella vulgaris

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