The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
The Cystathionine Pathway in the Silkworm Larva, Bombyx mori
YOSHIKAZU KONDO
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1962 年 51 巻 3 号 p. 188-192

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1. Paper chromatographic studies were made on the cystathionine-containing fraction obtained from silkworm and related insects. It was found that this amino acid was commonly present in the larval hemolymph of silkworm, including five races with white blood and one with yellow blood, but not in other Lepidopterous insects.
2. In silkworm larvae, S35 of injected methionine was converted to cystathionine, but not to cystine or to other sulfur-containing metabolite.
3. Antheraea pernyi having no cystathionine, on the other hand, catalyzed the conversion of S35-DL-methionine to S35-cystine, S35-taurine and, S35-sulfate.
4. From the above results, the accumulation of L-cystathionine in Bombyx mori larval hemolymph seems to be caused by an absence or very low activity of the cystathionine cleaving enzyme, cystathionase.
The author is indebted to Prof. M. Suda of the Institute for Protein Research, Osaka University for discussion and encouragement in this study.

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