Purification and Properties of Soluble and Bound [gamma]-Glutamyltransferases from Radish Cotyledon

Soluble and cell wall bound γ-glutamyltransferases (GGTs) were purified from radish (Raphanus sativus L.) cotyledons. Soluble GGTs (GGT I and II) had the same Mr of 63,000, and were composed of a heavy subunit (Mr, 42,000) and a light one (Mr, 21,000). The properties of GGT I and II were similar. Bo...

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Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-02, Vol.70 (2), p.369
Main Authors: NAKANO, Yoshihiro, OKAWA, Satoshi, YAMAUCHI, Takayoshi, KOIZUMI, Yukio, SEKIYA, Jiro
Format: Article
Language:English
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Summary:Soluble and cell wall bound γ-glutamyltransferases (GGTs) were purified from radish (Raphanus sativus L.) cotyledons. Soluble GGTs (GGT I and II) had the same Mr of 63,000, and were composed of a heavy subunit (Mr, 42,000) and a light one (Mr, 21,000). The properties of GGT I and II were similar. Bound GGTs (GGT A and B) were purified to homogeneity from the pellet after the extraction of soluble GGTs. GGT A and B were monomeric proteins with an Mr of 61,000. The properties of GGT A and B were similar. Thus, bound GGTs were distinguished from soluble GGTs. The optimal pHs of soluble and bound GGTs were about 7.5. Both soluble and bound GGTs utilized glutathione, γ-L-glutamyl-p-nitroanilide, oxidized glutathione and the conjugate of glutathione with monobromobimane as substrates, and were inhibited by acivicin, but soluble GGTs were also distinguished from bound GGTs with regard to these properties.
ISSN:0916-8451
1347-6947