Quantitative Analysis of Cytochrome C Released from Rice Mitochondria Using the Adsorptive Polarographic Wave of Guanidine Modified Co(II)- cytochrome C Complex
Abstract:A new, simple and sensitive method for the quantitative analysis of cytochrome C (Cyt C) based on the reduction wave of guanidine modified Co(II)-Cyt C complex at about -1.74 V (vs. SCE) by single sweep polarography in the solution containing 8'10-6 mol L-1 CoCl2, 0.04 mol L-1 guanidine hydrochloride, 0.2 mol L-1 NaOH and 0.5% Na2SO3. The peak height is linearly proportional to the concentration of Cyt C in the range of 0.005∼1.500 mg L-1 (correlation coefficient 0.999). Common amino acids, saccharide, organic acid and metal ions of appropriate concentrations have no interference on the Cyt C determination. The released Cyt C in the process of mitochondrial permeability transition of Hong-Lian cytoplasmic male sterile line of rice has been measured by the method, and the result is satisfactory.
Document Type: Research Article
Affiliations: Key Lab for Biotechnology of National Commission for Nationalities, 2College of Life Science, South- Central University for Nationalities, Wuhan 430074, P.R. China.
Publication date: August 1, 2006
More about this publication?
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.