Analysis of a Complex Antigenic Site on Horse Cytochrome c

1978 ◽  
pp. 119-129 ◽  
Author(s):  
Ronald Jemmerson ◽  
E. Margoliash
Keyword(s):  
Cytochrome C ◽  
Antigenic Site ◽  
Horse Cytochrome

scholarly journals The effect of complete or specific partial acetimidylation on the biological properties of cytochrome c and cytochrome c-T

1984 ◽  
Vol 217 (3) ◽  
pp. 595-599 ◽  
Author(s):  
C J A Wallace
Keyword(s):  
Structural Change ◽  
Cytochrome C ◽  
Oxygen Uptake ◽  
Redox Potential ◽  
Biological Properties ◽  
Amino Groups ◽  
Cytochromes C ◽  
Restricted Region ◽  
Horse Cytochrome

The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.

Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c

2015 ◽  
Vol 585 ◽  
pp. 52-63 ◽  
Author(s):  
Rishu Jain ◽  
Rajesh Kumar ◽  
Sandeep Kumar ◽  
Ritika Chhabra ◽  
Mukesh Chand Agarwal ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Folding Kinetics ◽  
Ph Dependent ◽  
Kinetics Of ◽  
Horse Cytochrome

scholarly journals A new non-covalent complex of semisynthetically modified tryptic fragments of cytochrome c

1986 ◽  
Vol 239 (2) ◽  
pp. 333-337 ◽  
Author(s):  
A E Proudfoot ◽  
C J Wallace ◽  
D E Harris ◽  
R E Offord
Keyword(s):  
Biological Activity ◽  
Cytochrome C ◽  
Redox Potential ◽  
Peptide Bond ◽  
Succinate Oxidation ◽  
Covalent Complex ◽  
Horse Cytochrome

We have prepared a semisynthetic analogue of fully acetimidylated horse cytochrome c, a complex in which the peptide bond between residues glycine-37 and arginine-38 is lacking. In contrast with the complex that we have previously described [Harris & Offord (1977) Biochem. J. 161, 12-25], in which the break in continuity is between residues arginine-38 and lysine-39, the new analogue has a nearly normal redox potential, and can more fully restore succinate oxidation to mitochondria depleted of cytochrome c. Studies of this and other analogues lead us to propose an explanation for the low biological activity of complex (1-38)-(39-104) and a role for the invariance of arginine-38.

Stereoselectivity in the oxidation of horse cytochrome c by tris(oxalato)cobaltate(3-)

1991 ◽  
Vol 30 (22) ◽  
pp. 4282-4285 ◽  
Author(s):  
Joel T. Ficke ◽  
Jack R. Pladziewicz ◽  
Eileen C. Sheu ◽  
A. Graham. Lappin
Keyword(s):  
Cytochrome C ◽  
Horse Cytochrome
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