The authors of the article “Purification of fat body glutathione S‐transferase from the desert locust Schistocerca gregaria : investigation of flavonoid inhibitory effects on enzyme activity”, published originally online on 9 June 2019, and subsequently on issue 44:3–4 of Physiological Entomology (pp. 187–199) [1], have alerted the journal of the following mistakes, found after publication:

Table 8 contained some incorrect values. The amended version of the table is shown below:

On page 190, it is stated:

Purification of GST from S. gregaria fat body .

DEAE‐Sepharose column chromatography . The enzyme homogenate prepared from fat body homogenate was applied on a DEAE‐Sepharose column previously equilibrated with 50 mM Tris‐HCl buffer (pH 8) (buffer A) and washed with the same buffer. The adsorbed proteins were eluted using a stepwise NaCl gradient ranging from 0.05 to 0.5 M.

GSH‐Sepharose affinity chromatography . Reduced glutathione (GSH) was coupled to epoxy activated Sepharose 6B as described by Simons & Vander‐Jagt (1977). DEAE‐Sepharose‐pooled fractions containing GST activity were dialyzed for 2 h against buffer A. The dialyzed samples were then applied to GSH‐Sepharose matrix previously equilibrated with buffer A and allowed to couple for 30 min at 4 °C with shaking. The homogeneity of the pooled material was analyzed by native polyacrylamide gel electrophoresis (PAGE) (7%) as described by Davis (1964). Visualization of GST activity was performed as described by Ricci et al. (1984). The SDS‐PAGE was performed using 12% (w/v) polyacrylamide gel (Laemmli, 1970). Protein bands were then visualized using Coomassie brilliant blue (R‐250) stain. The purified enzyme was stored at −20 °C.

This should read:

Purification of GST from S. gregaria fat body .

GSH‐Sepharose affinity chromatography . Reduced glutathione (GSH) was coupled to epoxy activated Sepharose 6B as described by Simons & Vander‐Jagt (1977). Fat body crude homogenate was applied on GSH‐Sepharose matrix previously equilibrated with 50 mM Tris–HCl buffer (pH 8) (buffer A) and allowed and allowed to couple for 30 min at 4 °C with shaking.

DEAE‐Sepharose column chromatography . GSH‐Sepharose pooled fractions containing GST activity were dialyzed for 2 h against buffer A. The dialyzed samples were then applied on DEAE‐Sepharose column previously equilibrated with buffer A and washed with the same buffer. The adsorbed proteins were eluted using a stepwise NaCl gradient ranging from 0.05 to 0.5 M. The homogeneity of the pooled material was analyzed by native polyacrylamide gel electrophoresis (PAGE) (7%) as described by Davis (1964). Visualization of GST activity was performed as described by Ricci et al . (1984). The SDS‐PAGE was performed using 12% (w/v) polyacrylamide gel (Laemmli, 1970). Protein bands were then visualized using Coomassie brilliant blue (R‐250) stain. The purified enzyme was stored at −20 °C.

Figure 6 of the article was accidently replaced by Fig. 5. The correct Fig. 6 is shown below:

On page 194, it is stated:

the enzyme reaction was increased from 3.13 μmol min⁻¹ mg protein⁻¹ (enzyme only) to 4 and 6.3 μmol min⁻¹ mg⁻¹ protein in the presence of delphinidin chloride and quercetin in the reaction medium (Figs. 5a and 6a). When CDNBwas the varied substrate, the same type of inhibition was observed when 3.88 μm of delphinidin chloride was used in the reaction medium (Fig. 6). Indeed, the inhibition type was found to be competitive for quercetin with CDNB and noncompetitive with GSH and it was noncompetitive with both CDNB and GSH for delphinidin chloride (Table 8).

This should read:

the enzyme reaction was decreased from 0.31 μmol min⁻¹ mg protein⁻¹ (enzyme only) to 0.16 and 0.25 μmol min⁻¹ mg⁻¹ protein in the presence of quercetin and delphinidin chloride in the reaction medium (Figs. 5a and 6a). When CDNBwas the varied substrate, the same type of inhibition was observed when 3.88 μm of delphinidin chloride was used in the reaction medium (Fig. 6). Indeed, the inhibition type was found to be competitive for quercetin with CDNB and noncompetitive with GSH and it was noncompetitive with both CDNB and GSH for delphinidin chloride (Table 8).

The authors apologize for these errors.

2019年6月9日在线发表，随后发表在《生理》杂志第44：3-4中的文章“从沙漠蝗虫日本血吸虫中纯化脂肪体谷胱甘肽S转移酶：研究类黄酮对酶活性的抑制作用”昆虫学（pp。187–199）[ 1 ]使期刊发现以下错误，这些错误是在出版后发现的：

表8包含一些不正确的值。该表的修订版本如下所示：

在页190，它指出：

紫花苜蓿脂肪体中GST的纯化。

DEAE-琼脂糖柱色谱法。由脂肪匀浆制备的酶匀浆应用于预先用50 mM Tris-HCl缓冲液（pH 8）（缓冲液A）平衡的DEAE-Sepharose柱上，并用相同的缓冲液洗涤。使用范围从0.05到0.5 M的逐步NaCl梯度洗脱吸附的蛋白质。

GSH-琼脂糖亲和色谱。如Simons＆Vander‐Jagt（1977）所述，还原型谷胱甘肽（GSH）与环氧活化的Sepharose 6B偶联。将含有GST活性的DEAE-Sepharose合并的级分对缓冲液A透析2 h。然后将透析后的样品应用于预先用A缓冲液平衡的GSH-Sepharose基质中，并于4°C振摇耦合30分钟。如Davis（1964）所述，通过天然聚丙烯酰胺凝胶电泳（PAGE）（7％）分析合并材料的均匀性。GST活性的可视化如Ricci等人所述进行。（1984）。SDS-PAGE使用12％（w / v）聚丙烯酰胺凝胶（Laemmli，1970）进行。然后使用考马斯亮蓝（R-250）染色剂对蛋白条带进行可视化。纯化的酶储存在-20℃。

内容应为：

紫花苜蓿脂肪体中GST的纯化。

GSH-琼脂糖亲和色谱。如Simons＆Vander‐Jagt（1977）所述，还原型谷胱甘肽（GSH）与环氧活化的Sepharose 6B偶联。将脂肪体粗匀浆应用于预先用50 mM Tris-HCl缓冲液（pH 8）（缓冲液A）平衡的GSH-琼脂糖基质上，使其在4°C振摇下偶联30分钟。

DEAE-琼脂糖柱色谱法。将含有GST活性的GSH-Sepharose合并级分对缓冲液A透析2 h。然后将透析后的样品加到事先用A缓冲液平衡过的DEAE-Sepharose柱上，并用相同的缓冲液洗涤。使用范围从0.05到0.5 M的逐步NaCl梯度洗脱吸附的蛋白质。如Davis（1964）所述，通过天然聚丙烯酰胺凝胶电泳（PAGE）（7％）分析合并材料的均一性。如Ricci等人所述进行GST活性的可视化。（1984）。SDS-PAGE使用12％（w / v）聚丙烯酰胺凝胶（Laemmli，1970）进行。然后使用考马斯亮蓝（R-250）染色剂对蛋白条带进行可视化。纯化的酶储存在-20℃。

文章的图6意外地被图5取代。正确的图6如下所示：

在页194上指出：

在反应培养基中存在氯化翠绿素和槲皮素的情况下，酶反应从3.13μmol·min ^-1  mg蛋白质^-1（仅酶）增加到4和6.3μmol·min ^-1  mg ^-1蛋白质（图5a和6a） 。当CDNB是变化的底物时，在反应介质中使用3.88μm的delphinidin chloride时，观察到相同类型的抑制作用（图6）。实际上，已发现抑制类型与槲皮素与CDNB竞争，而与GSH不竞争，而对CDNB和GSH则对delphinidin chloride具有竞争性（表8）。

内容应为：

在反应介质中存在槲皮素和delphinidin氯化物的情况下，酶反应从0.31μmol·min ^-1  mg蛋白质^-1（仅酶）降至0.16和0.25μmol·min ^-1  mg ^-1蛋白质（图5a和6a） 。当CDNB是变化的底物时，当在反应介质中使用3.88μm的delphinidin chloride时，观察到相同类型的抑制作用（图6）。实际上，已发现抑制类型与槲皮素与CDNB竞争，而与GSH不竞争，而对CDNB和GSH则对delphinidin chloride具有竞争性（表8）。

作者为这些错误表示歉意。