Impact of Some Avermectins on Lactoperoxidase in Bovine Milk

Zeynep KöksalDepartment of Chemistry, Faculty of Sciences, Atatürk University, Erzurum, Turkey;Department of Chemistry, Faculty of Sciences, İstanbul Medeniyet University, İstanbul, TurkeyView further author information

Ramazan KalınDepartment of Chemistry, Faculty of Sciences, Atatürk University, Erzurum, Turkey;Department of Basic Science, Faculty of Sciences, Erzurum Technical University, Erzurum, TurkeyView further author information

İlhami GülçinDepartment of Chemistry, Faculty of Sciences, Atatürk University, Erzurum, Turkey;Zoology Department, Fetal Programming of Diseases Research Chair, College of Science, King Saud University, Riyadh, Saudi ArabiaCorrespondence[email protected]
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Hasan ÖzdemirDepartment of Chemistry, Faculty of Sciences, Atatürk University, Erzurum, TurkeyView further author information

Ali AtaseverAtaturk University, Ispir Hamza Polat Vocational Training School, Erzurum, TurkeyView further author information

Figures & data

FIGURE 1 Chemical structures of some avermectins, including emamectin-benzoate, doramectin, eprinomectin, abamectin, moxidectin-vetranal, and ivermectin.

FIGURE 2 Sodium dodecylsulphate–polyacrylamide gel electrophoresis (SDS-PAGE) band of LPO. Column “c” is purified LPO from bovine milk by Sepharose 4B-L-Tyrosine sulphanilamide affinity column chromatography. Column “a” is standard proteins (Line 1: 250 kDa, Line 2: 150 kDa, Line 3: 100 kDa, Line 4: 70 kDA, Line 5: 50 kDA, Line 6: 40 kDA, Line 7: 30 kDA, Line 8: 20 kDa, Line 9: 15 kDa).

TABLE 1 Purification scheme for LPO obtained after the Amberlite CG-50 H⁺ resin and Sepharose 4B-L-tyrosine-sulphanamide affinity chromatography purification steps (LPO: Lactoperoxidase enzyme purified from bovine milk)

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TABLE 2 The half maximal inhibitory concentration (IC₅₀), inhibition constant (K_i), and inhibition type of avermectins against LPO purified from bovine milk by Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography (LPO: Lactoperoxidase)

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Impact of Some Avermectins on Lactoperoxidase in Bovine Milk

TABLE 1 Purification scheme for LPO obtained after the Amberlite CG-50 H⁺ resin and Sepharose 4B-L-tyrosine-sulphanamide affinity chromatography purification steps (LPO: Lactoperoxidase enzyme purified from bovine milk)

TABLE 2 The half maximal inhibitory concentration (IC₅₀), inhibition constant (K_i), and inhibition type of avermectins against LPO purified from bovine milk by Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography (LPO: Lactoperoxidase)

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Impact of Some Avermectins on Lactoperoxidase in Bovine Milk

Figures & data

TABLE 1 Purification scheme for LPO obtained after the Amberlite CG-50 H+ resin and Sepharose 4B-L-tyrosine-sulphanamide affinity chromatography purification steps (LPO: Lactoperoxidase enzyme purified from bovine milk)

TABLE 2 The half maximal inhibitory concentration (IC50), inhibition constant (Ki), and inhibition type of avermectins against LPO purified from bovine milk by Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography (LPO: Lactoperoxidase)

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TABLE 1 Purification scheme for LPO obtained after the Amberlite CG-50 H⁺ resin and Sepharose 4B-L-tyrosine-sulphanamide affinity chromatography purification steps (LPO: Lactoperoxidase enzyme purified from bovine milk)

TABLE 2 The half maximal inhibitory concentration (IC₅₀), inhibition constant (K_i), and inhibition type of avermectins against LPO purified from bovine milk by Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography (LPO: Lactoperoxidase)