B.c1 complex from beef heart: hydrodynamic properties of the complex prepared by a refined hydroxyapatite chromatography in trition X-100

Von Jagow, G.; Schägger, H.; Riccio, P.; Klingenberg, M.; Kolb, H.J.

Biochimica et Biophysica Acta 462(3): 549-558

1977


ISSN/ISBN: 0006-3002
PMID: 202306
DOI: 10.1016/0005-2728(77)90100-1
Accession: 068523880

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Abstract
The homogeneity and the MW of the Triton X-100. The isolation procedure is modified as compared to that described recently. The resulting preparation is devoid of the Fe S protein and contains more heme b (8.6 as compared to 8.0 .mu.mol/g protein). The sedimentation coefficient was determined to be s20,w = 13.03-13.09. Equilibrium runs observed at 415 and 280 nm exhibit straight curves (log c vs. r2) indicating that the preparation is homogeneous. After correction for bound Triton X-100, MW of 400,000-440,000 were calculated from the curves obtained at the respective wavelengths. From the heme contents a minimum MW of about 200,000 is calculated. The complex is present as a dimer. The average polarity of the whole complex as calculated from the amino acid analysis is relatively high (45%). In accordance with the high polarity the amount of bound detergent is relatively low; it amounts to 0.2 g Triton X-100/g protein. The amount of Triton bound to 1 mol of b-c1-dimer corresponds to the MW of the Triton micelle.