Literature DB >> 2540179

Determination of three disulfide bonds and one free sulfhydryl in the beta subunit of (Na,K)-ATPase.

T L Kirley1.   

Abstract

The oxidation state of the 7 cyst(e)ine residues of the beta subunit of lamb kidney (Na,K)-ATPase was determined. The fluorescent sulfhydryl-reactive reagent 4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole was utilized before and after reduction of disulfide bonds to determine the number and location of disulfide bonds present in the beta subunit. Treatment of tryptic peptides of the beta subunit separated by reverse phase high performance liquid chromatography with a reducing agent and 4-(aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole allowed identification of which residues were disulfide-linked. The results indicated that there is only one free sulfhydryl, Cys44, and that Cys125 is disulfide-bonded to Cys148, Cys158 is disulfide-linked to Cys174, and Cys212 is disulfide-bonded to Cys275. All three disulfide bonds were shown to be reduced in the presence of high concentrations of beta-mercaptoethanol and elevated temperature. These conditions also lead to a loss of (Na,K)-ATPase activity.

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Year:  1989        PMID： 2540179

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  14 in total

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Review 10.  Na,K-ATPase: isoform structure, function, and expression.

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