The structure of hemopeptide 1–65 from cytochrome c

Hemopeptide 1–65 was cleaved from horse heart cytochrome c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no sig...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1972, Vol.148 (1), p.141-147
Hauptverfasser:	Babul, Jorge, McGowan, Eleanor B., Stellwagen, Earle
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetates Alkylation Amino Acids - analysis Animals Bromine Chemical Phenomena Chemistry, Physical Chromatography, Gel Circular Dichroism Cyanogen Bromide Cytochromes - analysis Heme - analysis Histidine Horses Myocardium Peptides - analysis Peptides - isolation & purification Potassium Iodide Protein Binding Protein Conformation Spectrophotometry Ultracentrifugation Ultraviolet Rays Viscosity
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