19246-18-5Relevant articles and documents
-
Loring,du Vigneaud
, p. 385,387 (1935)
-
Molecular cloning and characterization of γ-Glutamyltranspeptidase from pseudomonas nitroreducens IFO12694
Imaoka, Masashi,Yano, Shigekazu,Okumura, Masashi,Hibi, Takao,Wakayama, Mamoru
experimental part, p. 1936 - 1939 (2011/06/11)
y-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydro-lytic activity than transfer activity, as compared with other y-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard y-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a y-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.
Purification and properties of soluble and bound γ- glutamyltransferases from radish cotyledon
Nakano, Yoshihiro,Okawa, Satoshi,Yamauchi, Takayoshi,Koizumi, Yukio,Sekiya, Jiro
, p. 369 - 376 (2008/02/10)
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.