EurekaMag.com logo
+ Site Statistics
References:
52,725,316
Abstracts:
28,411,598
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Preparation of mono specific antibodies against 2 forms of rat liver cytochrome p 450 and quantitation of these antigens in microsomes


Archives of Biochemistry & Biophysics 192(2): 524-532
Preparation of mono specific antibodies against 2 forms of rat liver cytochrome p 450 and quantitation of these antigens in microsomes
Antibodies prepared against purified cytochrome P-450 and P-448 from phenobarbital- and 3-methylcholanthrene-pretreated rats recognize several forms of hepatic cytochrome P-450. These antibodies were made monospecific for a single form of cytochrome P-450 by immunoadsorption with partially purified solid-phase cytochrome P-450 from rats treated with a different inducer than that used for isolation of the antigen. Each monospecific antibody did not react with different forms of cytochrome P-450 present in the heterologous antigen preparation. These monospecific antibodies, covalently bound to Sepharose, were used to purify the antigens (catalytically inactive) from microsomes in a single step. The high specificity of these antibodies for a single form of cytochrome P-450 was used to quantitate 2 forms of cytochrome P-450 in rat liver microsomes by radial immunodiffusion. The percentage of the total cytochrome P-450 in microsomes that is represented by each of these 2 forms of cytochrome P-450 varied from 3-89% depending on the xenobiotic pretreatment of the rats.


Accession: 006173501



Related references

Preparation of monospecific antibodies against two forms of rat liver cytochrome P-450 and quantitation of these antigens in microsomes. Archives of Biochemistry and Biophysics 192(2): 524-532, 1979

Sex difference of cytochrome P-450 in the rat: purification, characterization, and quantitation of constitutive forms of cytochrome P-450 from liver microsomes of male and female rats. Archives of Biochemistry and Biophysics 225(2): 758-770, 1983

Quantitation of different forms of cytochrome p 450 from 3 methyl cholanthrene treated rats and from pheno barbital treated rats with mono specific antibodies. Federation Proceedings 38(3 PART 1): 526, 1979

Immunochemical quantitation of 3 forms of cytochrome p 450 in liver microsomes of rats treated with several inducers. Federation Proceedings 39(6): ABSTRACT 1800, 1980

Quantitation of multiple forms of cytochrome p 450 hemo proteins fluorescence gel scanning of rat liver microsomes. Pharmacologist 20(3): 181, 1978

Purification and characterization of three male-specific and one female-specific forms of cytochrome P-450 from rat liver microsomes. Journal of Biochemistry 100(5): 1359-1371, 1986

Pituitary regulation of sex-specific forms of cytochrome P-450 in liver microsomes of rats. Biochemical and Biophysical Research Communications 130(3): 1247-1253, 1985

Decrease in the specific forms of cytochrome P-450 in liver microsomes of a mutant strain of rat with hyperbilirubinuria. Research Communications in Chemical Pathology and Pharmacology 72(2): 243-253, 1991

Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography. Archives of Biochemistry and Biophysics 265(1): 159-170, 1988

Ascorbic acid deficiency decreases specific forms of cytochrome P-450 in liver microsomes of guinea pigs. Molecular Pharmacology 39(4): 456-460, 1991