Methabolism and functional role of D-aspartic acid and related compounds in marine animals.
Project/Area Number |
01560228
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Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
Fisheries chemistry
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Research Institution | Tohoku University (1990-1991) Kitasato University (1989) |
Principal Investigator |
SATO Minoru Tohoku University Faculty of Agriculture Associate Professor, 農学部, 助教授 (70050680)
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Project Period (FY) |
1989 – 1990
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Project Status |
Completed (Fiscal Year 1991)
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Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1990: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1989: ¥1,500,000 (Direct Cost: ¥1,500,000)
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Keywords | D-amino acid / D-aspartate / B-D-aspartylglycine / distribution / metabolism / physiological function / NーメチルーDーアスパラギン酸 / βーDーAsp・gly / HPLC分析 / D-アミノ酸 / D-アスパラギン酸 / N-メチル-D-アスパラギン酸 / β-D-Asp・gly |
Research Abstract |
D-amino acids, which were viewed as natural oddities, have recently been found in various animals, plants and bacteria. In marine invertebrates it has been noted that D-alanine occurs in octopus muscle and D-aspartic acid(D-asp)in the nervous tissue of the cephalopods, Loligo, Sepia and Octopus. D-am'lno acids have also been reported in crustaceans, polychastes and bivalves. . These reports are however fragmentary studies, and the metabolism and the functional role of these D-amino acids are not known. This study was aimed to obtain the basic information on the distribution, metabolism and physiological function of D-amino acids especially D-asp in marine animals. On the course of the survey for the presence of free D-asp, an unknown large peak was found on the HPLC chromatogram of Aplysia kurodai- extract. It was isolated by ion-exchange chromatography using Dowex I and 50, and preparative high voltage paper electrophoresis and obtained as crystal. It was shown by optical rotatory dispersion spectrum and optical-resolusion HPLC analysis that this compound was consisted of equimolar amounts of Dasp and glycine. This compound resisted to the Edman's cleavage. This peptide was inferred to be beta-D-aspartylglycine and confirmed by synthesis. Thirty two species of marine animals were surveyed for the presence of free D-asp in their tissues. D-asp was found in all marine animals investigated. In marine invertebrates, D-asp occurred at levels of 20-60% of total Asp(D+L-form). Trace amount of D-asp was also detected in vertebrate(fish). Contrary, beta-aspartylglycine was detected only in Aplysia kurodai and A. juliana. Concerning the metabolism of D-asp in bivalve Mytilus e u is, the enzyme alanine oxaloacetate transaminase could be shown to be present in the mid-gut gland but not D-asp racemase or D-aspartate oxidase. L-alanine is most effective amino group donner to oxaloacetate to synthesis of D-asp in the tissue of M. edulis.
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Report
(3 results)
Research Products
(4 results)