Nine distinct monoclonal antibodies raised against purified rat liver cytochrome P-450c react with six different epitopes on the antigen, and one of these epitopes is shared by cytochrome P-450d. None of these monoclonal antibodies recognize seven other purified rat liver isozymes (cytochromes P-450a, b, and e-i) or other proteins in the cytochrome P-450 region of "Western blots" of liver micro...

An important role in ensuring the functioning of respiratory chain belongs to cytochrome part, which includes complexes III (ubiquinol-cytochrome c oxidoreductase) and IV (cytochrome oxidase). The key components these enzymatic are heme-containing cytochromes, number depends on balance heme synthesis catabolism. δ-Aminolevulinate synthase catalyzes first step biosynthetic pathway, while oxygena...

Mammals express multiple cytochromes P450 simultaneously in a variety of tissues, including the liver, kidney, lung, adrenal, gonads, brain, and most others. For cytochromes P450 that are expressed in many tissues or cell types, the tissue/cell type-specific expression might be associated with their special physiological roles. Several cytochrome P450 enzymes are found not only in different cel...

This paper presents a nonivasive approach to study redox state of reduced cytochromes c, c1 and b of complexes II and III in mitochondria of live cardiomyocytes by means of Raman microspectroscopy. For the first time with the proposed approach we perform studies of rod- and round-shaped cardiomyocytes, representing different morphological and functional states. Raman mapping and cluster analysi...

1. Spectrophotometric analysis of intact cells of Schizosaccharomyces pombe, harvested from exponentially growing cultures during the phase of glucose repression, revealed thepresence ofcytochromesa+a3, cand at least two species of cytochrome b. 2. An absorption maximum at 554nm at 77°K, previously attributed to cytochrome cl, has been identified as a b-type cytochrome. 3. CO-difference spectra...

The formal potential of c-type cytochromes expressed in the bacterial outer membrane was dependent on their redox state functioning in mediating extracellular electron transfer. Its negative (positive) shifting accompanying with the oxidization (reduction) of c-type cytochromes can serve to stabilize the redox states in a feedback manner.