Identification of Malonylation, Succinylation, and Glutarylation in Serum Proteins of Acute Myocardial Infarction Patients

Purpose To identify protein malonylation, succinylation, and glutarylation in human and rat serum. Experimental design Immunoprecipitation coupled with MS/MS is employed to compare the relative abundance of malonylation, succinylation, and glutarylation of serum protein in acute myocardial infarctio...

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Bibliographic Details
Published in:Proteomics. Clinical applications 2020-01, Vol.14 (1), p.e1900103-n/a
Main Authors: Zhou, Boda, Du, Yipeng, Xue, Yajun, Miao, Guobin, Wei, Taotao, Zhang, Ping
Format: Article
Language:English
Subjects:
Albumins
Design of experiments
Electrocardiography
Experimental design
glutarylation
Heart attacks
Immunoprecipitation
malonylation
Myocardial infarction
Peptides
Proteins
Relative abundance
Serum proteins
succinylation
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Summary:Purpose To identify protein malonylation, succinylation, and glutarylation in human and rat serum. Experimental design Immunoprecipitation coupled with MS/MS is employed to compare the relative abundance of malonylation, succinylation, and glutarylation of serum protein in acute myocardial infarction human and rat. Results One hundred thirty and 48 unique malonylated, succinylated, or glutarylated peptides are found in human and rat serum, respectively. Succinylation is the most predominant modification. The most modified protein is albumin. Abundance of serum protein succinylation and glutarylation is significantly (p 
ISSN:1862-8346
1862-8354
DOI:10.1002/prca.201900103