Acetylation and glycation of fibrinogen in vitro occur at specific lysine residues in a concentration dependent manner: A mass spectrometric and isotope labeling study

Biochemical and Biophysical Research Communications

Volumn 421, Issue 2, 2012, Pages 335-342

  Svensson, Jan ^a,b   Bergman, Ann Charlotte ^a   Adamson, Ulf ^b   Blombäck, Margareta ^a   Wallén, Håkan ^b   Jörneskog, Gun ^b  

^a KAROLINSKA UNIVERSITY HOSPITAL   (Sweden)

^b DANDERYD HOSPITAL   (Sweden)

Author keywords

Acetylation; Aspirin; Fibrinogen; Glycation; Lysine; Mass spectrometry

Indexed keywords

ACETYLSALICYLIC ACID; BLOOD CLOTTING FACTOR 13; CARBON 14; FIBRINOGEN; GLUCOSE; LYSINE;

ACETYLATION; ALPHA CHAIN; ANALYTIC METHOD; ARTICLE; BETA CHAIN; BINDING COMPETITION; CONCENTRATION RESPONSE; CROSS LINKING; DIABETES MELLITUS; GLYCATION; IN VITRO STUDY; ISOTOPE LABELING; MASS SPECTROMETRY; PRIORITY JOURNAL;

ACETYLATION; AMINO ACID SEQUENCE; ASPIRIN; FIBRINOGEN; FIBRINOLYTIC AGENTS; GLUCOSE; GLYCOSYLATION; ISOTOPE LABELING; LYSINE; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY;

EID: 84860494225     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.154     Document Type: Article

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