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

Spectrophotometric evidence for a hemoprotein in fish muscle microsomes possible involvement in trimethylamine n oxide tmao demethylase activity


Journal of Agricultural & Food Chemistry 35(1): 34-41
Spectrophotometric evidence for a hemoprotein in fish muscle microsomes possible involvement in trimethylamine n oxide tmao demethylase activity
When fish muscle microsomes were reduced with sodium dithionite, characteristic absorption peaks appeared at 444 nm and very faintly at 560 nm. These peaks could also be generated by the presence of some of the components that are required for catalyzing microsomal enzyme-mediated trimethylamine N-oxide (TMAO) demethylation. Under certain conditions, the aborbance peaks underwent reoxidation in the presence of these cofactor components and TMAO. The reducible moiety was identified as protoheme by virtue of its absorption maxima at 557, 532, and 416 nm following solubilization in acid-acetone and reaction with pyridine, and it is proposed that it be named H-444 due to its unique Soret band. Reaction of the microsomes with CO after reduction with dithionite produced a Soret band shift from 444 to 428 nm. The hemin content of the fish muscle microsomes was 0.76 pmol mg-1 protein, some 3 orders of magnitude less than that observed in hepatic microsomes. This microsomal hemoprotein may possibly be involved in TMAO demethylation.


Accession: 006460658



Related references

Characterization of trimethylamine-N-oxide (TMAO) demethylase activity from fish muscle microsomes. Journal of Biochemistry 100(1): 77-86, 1986

Partial purification of trimethylamine-N-oxide (TMAO) demethylase from crude fish muscle microsomes by detergents. Journal of Biochemistry 100(1): 87-97, 1986

Characterization of trimethylamine n oxide demethylase activity from fish muscle microsomes. Journal of Biochemistry (Tokyo) 100(1): 77-86, 1986

Distribution and some characteristics of trimethylamine N-oxide (TMAO) demethylase activity of red hake muscle. Journal of food biochemistry 17(4): 235-250, 1994

Identification and characterization of trimethylamine N-oxide (TMAO) demethylase and TMAO permease in Methylocella silvestris BL2. Environmental Microbiology 16(10): 3318-3330, 2015

Partial purification of trimethylamine n oxide demethylase from crude fish muscle microsomes by detergents. Journal of Biochemistry (Tokyo) 100(1): 87-98, 1986

Trimethylamine n oxide tmao demethylation and protein denaturation in fish muscle. Flick, G J Jr And R E Martin (Ed ) Advances in Seafood Biochemistry: Composition And Quality; American Chemical Society Annual Meeting on Biochemistry Of Seafood Products, New Orleans, Louisiana, Usa Xi+406p Technomic Publishing Co , Inc : Lancaster, Pennsylvania, Usa; Basel, Switzerland Illus 25-42, 1992

Relevance of trimethylamine oxide demethylase activity and haemoglobin content to formaldehyde production and texture deterioration in frozen stored minced fish muscle. Journal of the science of food and agriculture3(3): 261-276, 1988

Evaluation of freshness of fish products by determination of total volatile basic nitrogen (TVBN), trimethylamine (TMA), trimethylamine oxide (TMAO) and hypoxanthine. Veterinaria Italiana 34(27/28): 69-74, 1998

Trimethylamine n oxide demethylase tmao ase of saithe pollachius virens kidney a study of some physicochemical and enzymic properties. Journal of the Science of Food & Agriculture 59(2): 261-267, 1992