The isolation and properties of microsomal cytochrome.
نویسندگان
چکیده
Mammalian liver contains a heme protein which from its spectrum and properties in particulate preparations has been termed cytochrome b, by Yoshikawa (I), cytochrome m by C. F. Strittmatter and Ball, who localized it in microsomes (2,3), and cytochrome bg by Chance and Williams (4). In view of the fact that this and other microsomal enzymes have been studied chiefly in particulate suspensions, methods of isolating microsomal proteins for more detailed characterization were examined. The first and most easily recognizable of the enzymes that we have obtained is the microsomal cytochrome. This paper deals with the liberation of the cytochrome from its particulate complex, the fractionation steps in its purification, electrophoretic and ultracentrifugal tests for homogeneity, molecular weight determination, spectral properties, and reactions with a number of reagents.
منابع مشابه
The purification and properties of microsomal cytochrome reductase.
In earlier work (1) a DPNH’-specific microsomal cytochrome reductase, liberated by alcohol extraction and partially purified, was identified in liver microsome fractions from rats and rabbits. Microsomal cytochrome, but not cytochrome c, was found to act as electron acceptor in the oxidation of DPNH catalyzed by the enzyme. Through a rapid cytochrome to cytochrome reaction, cytochrome c was red...
متن کاملThe oxidation-reduction stoichiometry and potential of microsomal cytochrome.
In the preceding report (1) we have described the isolation, as an acidic protein of relatively low molecular weight, of the cytochrome component of rabbit liver microsomes. Of the various mammalian cytochromes, known from their spectra in crude preparations or intact cells, only cytochrome c has been previously isolated in a form which has permitted molecular characterization (24). Two propert...
متن کاملMICROSOME-MEDIATED BENZO[A]PYRENE-DNA BINDING AND INHIBITION BY CYTOSOLIC FRACTIONS FROM LIVER AND SKIN OF ADULT AND WEANLING RATS
Biotransformation of benzo[a]pyrene (BaP) in the presence of microsomal fractions derived from liver and epiderm of adult and weanling rats was examined. The aim of this study was to evaluate the effect of age on the capacity of two organs in transformation of BaP. Subcellular fractions were prepared from skin and liver by ultracentrifugation and were used as the source of BaP metabolizing enzy...
متن کاملThe nature of the heme binding in microsomal cytochrome b5.
In earlier work (2, 3) the isolation, physical properties, and chemical reactions of rabbit liver microsomal cytochrome bs were described. The nature of heme’ binding in this heme protein has now been examined with calf liver microsomal cytochrome bs. This first involved the preparation of undenatured apocytochrome b5 and the apoprotein of an iodinated and acetylated derivative of cytochrome b5...
متن کاملHepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization, and kinetic studies.
has previously been isolated by Horecker (1) from an acetone powder of liver and characterized as a flavoprotein. It was initially suggested that this enzyme was localized in hepatic mitochondria. However, subsequent studies have revealed that triphosphopyridine nucleotide-cytochrome c reductase activity is also present in hepatic microsomes (a), and it has been reported that the properties of ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 221 1 شماره
صفحات -
تاریخ انتشار 1956