Cytochrome C Isolation From Beef Heart Lab
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Periodical Article
The isolation and purification of cytochrome c1 from bovine heart [1980]
Koenig, B.Westward.; Schilder, L.T.M.; Tervoort, One thousand.J.; Gelder, B.F. van (Amsterdam Univ. (Netherlands). BCP Jansen Inst., Lab. voor Biochemie);
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The isolation and purification of cytochrome c1 from bovine heart
1980
A big-scale isolation method for cytochrome c(,1) from beefiness center is presented, based in principle on the procedure of Yu et al. (Yu, C.A., Yu, L. and King, T.Eastward. (1972) J. Biol. Chem. 247, 1012-1019). Optimal solubilization of cytochrome c(,i) from succinate-cytochrome c oxidoreductase was achieved with 15 per centBeta-mercaptoethanol, 1.five per cent cholate, 0.5 per cent deoxycholate in viii per cent saturated ammonium sulphate. The poly peptide is purified to a higher degree past chromatography on DEAE-cellulose and Ultrogel AcA 44. The method is reproducible and gives highly purified cytochrome c(,1) with a yield from succinate-cytochrome c oxidoreductase of twoscore per cent. The purified cytochrome c(,i) contains 32 nmol of heme/mg protein and has a spectral heme-to-poly peptide ratio (A('scarlet)(,417nm)/Air-conditioning'ox)(,276nm) of 2.7. Reduced cytochrome c(,ane) is oxidized very quickly by ferricytochrome c (kappa = 3x10E7/Yard/S at 10 deg C, 100 mM potassium phosphate (pH 7.0) and ane per cent Tween 20). Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate shows that the isolated poly peptide consists of 1 peptide, with a molecular weight of 31 000, carrying the chromophore. In the presence of i per cent sodium cholate or 1 per cent Tween 80, cytochrome c(,1) is in the monomeric land, whereas at lower concentrations of detergent the protein aggregates. The assemblage of cytochrome c(,i) is found to exist reversible
[Biochimica et Biophysica Acta - Protein structure (Netherlands)]
1980/XE/XE1980_0.rdf
A large-scale isolation method for cytochrome c(,one) from beef eye is presented, based in principle on the procedure of Yu et al. (Yu, C.A., Yu, 50. and King, T.East. (1972) J. Biol. Chem. 247, 1012-1019). Optimal solubilization of cytochrome c(,1) from succinate-cytochrome c oxidoreductase was accomplished with 15 per centBeta-mercaptoethanol, 1.5 per cent cholate, 0.v per cent deoxycholate in 8 per cent saturated ammonium sulphate. The protein is purified to a college degree by chromatography on DEAE-cellulose and Ultrogel AcA 44. The method is reproducible and gives highly purified cytochrome c(,1) with a yield from succinate-cytochrome c oxidoreductase of twoscore per cent. The purified cytochrome c(,1) contains 32 nmol of heme/mg protein and has a spectral heme-to-protein ratio (A('reddish)(,417nm)/Air-conditioning'ox)(,276nm) of two.7. Reduced cytochrome c(,1) is oxidized very rapidly by ferricytochrome c (kappa = 3x10E7/M/Due south at ten deg C, 100 mM potassium phosphate (pH seven.0) and 1 per cent Tween xx). Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate shows that the isolated protein consists of one peptide, with a molecular weight of 31 000, conveying the chromophore. In the presence of 1 per cent sodium cholate or 1 per cent Tween lxxx, cytochrome c(,1) is in the monomeric state, whereas at lower concentrations of detergent the protein aggregates. The aggregation of cytochrome c(,1) is found to be reversible
Biochimica et Biophysica Acta - Protein construction (Netherlands)
Bibliographic information
All titles:
"The isolation and purification of cytochrome c1 from bovine heart"@eng
Bibliographic information
All titles:
"The isolation and purification of cytochrome c1 from bovine heart"@eng
Source: https://agris.fao.org/agris-search/search.do?recordID=XE8080508
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