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Eisenia bicyclis, Arame, was allowed to photosynthesize in seawatercontaining H14CO3, and 14C-mannitol was isolated fromits fronds. The ratio of 14C-total/14C1 + 14C6 in the 14C-mannitolwas found to be about 8.0 at 1 min-illumination, but graduallydecreased with time to 3.0, showing uniform radioactivity distribution.Mannitol therefore seems to be formed in brown algae throughthree carbon compounds. Enzymes which may be involved in the possible biosynthetic pathwayof mannitol, i.e. aldolase, hexose diphosphatase, mannitol-1-phosphataseand glucosephosphate isomerase were present in extracts fromseveral brown algae. Some of their properties are discussed.
1Contribution from the Shimoda Marine Biological Station ofTokyo Kyoiku University, No. 187.
2Present address: Reseach Institute, Seikagaku Kogyo Co., Ltd.,Yamato-machi, Kitatama-gun, Tokyo, Japan. (Received December 13, 1968; ) 相似文献
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When the fronds of Eisenia bicyclis were exposed to H14CO3in the light, the radioactive carbon was rapidly incorporatedinto mannitol. Even after illumination of such a short periodas 5 min, about seventy percent of the total radioactivity incorporatedwas found in this compound, and the specific radioactivity ofthis alcohol decreased very rapidly during the subsequent darkincubation. Among various cellular polysaccharides examined,only laminaran showed a similar quick response with respectto the specific radioactivity change. On the basis of thesefindings it was concluded that mannitol and laminaran form storagesubstances in the brown alga, and they are possibly interchangeableas sucrose and starch do in higher plants.
1This work was partly reported at the 27th Annual Meeting ofthe Botanical Society of Japan, Nagoya, 1962, and at the 28thAnnual Meeting of the Botanical Society of Japan, Okayama, 1963.
2Contribution from the Shimoda Marine Biological Station, TokyoKyoiku University, No. 149. 相似文献
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NAGASHIMA HIDEYUKI; NAKAMURA SAHEYE; NISIZAWA KAZUTOSI; HORI TERUZO 《Plant & cell physiology》1971,12(2):243-253
ADP-glucose: -l,4-glucan -4-glucosyltransferase was obtainedfrom a marine red alga Serraticardia maxima in a form boundwith floridean starch granules. The enzyme catalyzed the transferof glucosyl residue from ADP-glucose, UDP-glucose and GDP-glucoseto floridean starch added as a primer. ADP-glucose was the mostefficient glucosyl donor in the reaction. Maltose was producedby ß-amylolysis of the glucan synthesized by the algalenzyme. The optimum pH for enzyme activity was at 8.4. The enzymewas not obtained in a soluble form from either the chloroplastextract or the whole algal cell extract. Electron micrographsof algal cells revealed that floridean starch granules are localizedexclusively outside chloroplasts. Hence, it appears that mostof the synthetase is present outside chloroplasts.
1 Contribution from the Shimoda Marine Biological Station, TokyoKyoiku University, No. 202. This work was supported by a Grant-in-Aidfor Cooperative Research from the Ministry of Education, Japan.
2 Present address: Department of Biology, Faculty of Science,Science University of Tokyo, Kagurazaka, Tokyo 162, Japan.
3 Present address: Laboratory of Biology, Faculty of Science,Toho University, Narashino, Chiba 275, Japan. (Received May 25, 1970; ) 相似文献
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The occurrence of a phosphorylase in the extracts of a greenseaweed, Ulva pertusa was demonstrated. In addition, a sugarphosphatase different from non-specific acid phosphatase andan amylase, which are involved in the starch degradation, werealso detected in this sea-lettuce.
1Contributions from the Shimoda Marine Biological Station, No.147. 相似文献
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