萝卜子叶中可溶性和结合性γ-谷氨酰转移酶的纯化及性质
Purification and properties of soluble and bound gamma-glutamyltransferases from radish cotyledon.
作者信息
Nakano Yoshihiro, Okawa Satoshi, Yamauchi Takayoshi, Koizumi Yukio, Sekiya Jiro
机构信息
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.
出版信息
Biosci Biotechnol Biochem. 2006 Feb;70(2):369-76. doi: 10.1271/bbb.70.369.
Soluble and cell wall bound gamma-glutamyltransferases (GGTs) were purified from radish (Raphanus sativus L.) cotyledons. Soluble GGTs (GGT I and II) had the same M(r) of 63,000, and were composed of a heavy subunit (M(r), 42,000) and a light one (M(r), 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 M(r) 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, gamma-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.
从萝卜（Raphanus sativus L.）子叶中纯化出了可溶性和细胞壁结合型γ-谷氨酰转移酶（GGTs）。可溶性GGTs（GGT I和II）的相对分子质量（M(r)）均为63,000，由一个重亚基（M(r)为42,000）和一个轻亚基（M(r)为21,000）组成。GGT I和II的性质相似。在提取可溶性GGTs后，从沉淀中纯化出了结合型GGTs（GGT A和B），使其达到了均一性。GGT A和B是相对分子质量为61,000的单体蛋白。GGT A和B的性质相似。因此，结合型GGTs与可溶性GGTs不同。可溶性和结合型GGTs的最适pH约为7.5。可溶性和结合型GGTs均以谷胱甘肽、γ-L-谷氨酰-p-硝基苯胺、氧化型谷胱甘肽以及谷胱甘肽与单溴代联苯胺的缀合物作为底物，且均被阿西维辛抑制，但在这些性质方面，可溶性GGTs也与结合型GGTs不同。
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