カイコのアミノ基転位反応及びグリオキシル酸生成系
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概要
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(1) The activity of glutamic-alanine and glutamic-aspartic transaminases was determined in the body fluid, the silk gland, the alimentary canal and the body wall of the silkworm at successive stages of metamorphosis. No activity of the enzymes was found in the body fluid. In other tissues the highest activity ofthe enzymes was detected on the 4th and 5th day of the last larval instar. Evenat the pupal stage when the activity was lowest, a considerable activity of theenzymes was found in the body wall, and a slight rise took place in activity atthe emergence. According to the calculation of the data obtained in larval tissue extracts, about 5 grams of amino-group were transfered in the last larval instar. The ratio of glutamic-alanine to glutamic-aspartic transaminase activity isabout 2.4 in the silk gland, 1.0 in the alimentary canal and 0.5 in the body wall through the larval stage. (2) In the exchange of the leaves of Morus bombycis, which is the most normal food for silkworms, for the leaves of Cudrania cochinchinensis var. gerontogea on and after the beginning of the last larval instar, the retardation for about one day was abserved until the highest activity of theenzymes was shown. As there was no difference in the nutritive quality evaluated from the yielding of the silk cocons between the leaves of both species, it was concluded that the above mentioned changes of the enzymatic activity did not become the limiting factor of the silk synthesis. (3) Enzymatic and non-enzymatictransaminations with α-keto acid and various amino acid were analysed by paperchromatographic technique. In the presence of cupric, ferric magnesium and alminium ions, that is, even in the boiled extracts of larval tissues non-enzymatic transamination with glyoxylic acid and various amino acid was abserved. This reaction was inhibited completely with disodium salt of ethylen diamine tetra acetic acid in very low concentration. On the other hand no transamination with phenylpyruvic acid and amino acid was observed. (4) Paper electrophoretic separation of the transaminases in the protein mixture of tissue extracts was studied in the following conditions: veronal buffer, pH 8-8.6, μ=0.05; run for 8 hours, at 5℃, 0.8V/cm. At the completion of the run the enzymatic activity was detected on 0.5cm segments of filter paper. The active protein was present in a fast migrating fraction, though the activity was reduced by one fifth during electrophoresis. (5) Glyoxylic acid formation from glycolic acid in tissue extracts was studied. As the tissue extracts showed the malic dehydrogenase activity, with sodium malate as substrate, diphosphopyridine nucleotide (DPN) was reduced. From the fact that the addition of sodium glyoxylate reoxidized the reduced DPN, it was identified that glycolic acid is one of the sources of glyoxylic acid in silkworm.
- 社団法人日本動物学会の論文
- 1961-09-15
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