Proteomic analysis of pooled and individual preparations of human liver microsomes

Published: 3 June 2024| Version 1 | DOI: 10.17632/znnw9kgy3n.1
Contributors:
,
,
, Dmitri Davydov

Description

Results of proteomic quantitation of cytochromes P450 and other drug-metabolizing and ER-stress-related proteins in pooled and individual preparations of human liver microsomes. The fractional content of 11 major cytochrome P450 species was determined with targeted proteomics in 14 pooled mixed gender HLM preparations obtained from commercial suppliers. Nine of these preparation along with the set of 23 individual HLM samples was also analyzed by untargeted total protein proteomics approach. The individual HLM samples were obtained from donors with different documented degree of alcohol exposure. The dataset contains the raw MS counts for 75 microsomal proteins and results of their analysis in terms of relative abundance of each protein and relative fractional content of cytochromes P450.

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Institutions

Washington State University

Categories

Biochemistry, Proteomics, Drug Metabolism

Funding

National Institute on Alcohol Abuse and Alcoholism

R01AA030155

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