Purification and Properties of Soluble and Bound γ-Glutamyltransferases from Radish Cotyledon
Purification and Properties of Soluble and Bound γ-Glutamyltransferases from Radish Cotyledon
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萝卜子叶可溶性和结合型γ-谷氨酰转移酶的纯化及性质
DOI：
10.1271/bbb.70.369
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
J. Sekiya
中科院分区：
文献类型：
--
作者：
Y. Nakano;S. Okawa;Takayoshi Yamauchi;Yukio Koizumi;J. Sekiya
从萝卜（Raphanus sativus L.）子叶中纯化出可溶性和细胞壁结合的γ-谷氨酰基转移酶（GGTs）。可溶性GGT （GGT I和GGT II）的mrr相同，均为63,000，由一个重亚基（mr4, 42,000）和一个轻亚基（mr2, 21,000）组成。GGT I和GGT II的性质相似。提取可溶性GGT后，将结合的GGT （GGT A和GGT B）从球团中纯化至均质。GGT A和GGT B为单体蛋白，mrr为61000。GGT A和GGT B的性质相似。因此，将结合型ggt与可溶性ggt区分开来。可溶性和结合型ggt的最佳ph值约为7.5。可溶性和结合性ggt均以谷胱甘肽、γ- l-谷氨酰-对硝基苯胺、氧化谷胱甘肽和谷胱甘肽与单溴茂烷的缀合物为底物，并受到acivicin的抑制，但可溶性ggt与结合性ggt在这些性质上也有所区别。
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 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, 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.
影响因子：
2.9
作者：
HANIGAN, MH;RICKETTS, WA
通讯作者：
RICKETTS, WA
肾γ-谷氨酰转肽酶：糖基化对其亚基的电泳行为和分子量的影响。
DOI：
10.1016/s0006-291x(86)80170-x
发表时间：
1986
影响因子：
3.1
作者：
Tate,SS;Khadse,V
通讯作者：
Khadse,V
DOI：
10.1073/pnas.93.15.7923
发表时间：
1996-07-23
影响因子：
11.1
作者：
Lieberman, MW;Wiseman, AL;Matzuk, MM
通讯作者：
Matzuk, MM