Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI–TOF MS-Reference-Cited by-同舟云学术

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Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI–TOF MS

Published:2011-08 Issue:17-18 Volume:412 Page:1606-1615
ISSN:0009-8981
Container-title:Clinica Chimica Acta
language:en
Short-container-title:Clinica Chimica Acta

Author:

Barnaby Omar S.,Cerny Ronald L.,Clarke William,Hage David S.

Funder

National Institute of Health

National Cancer Institute

Nebraska Research Initiative

Publisher

Elsevier BV

Subject

Biochemistry (medical),Clinical Biochemistry,Biochemistry,General Medicine

Reference45 articles.

1. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose;Thornalley;Biochem J,1999

2. Advanced glycation end products (AGE)-modified proteins and their potential relevance to atherosclerosis;Horiuchi;Trend Cardiovasc Med,1996

3. Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging;Araki;J Biol Chem,1992

4. Chemistry of browning reactions in model systems;Hodge;J Agric Food Chem,1953

5. Report on the expert committee on the diagnosis and classification of diabetes mellitus;Gavin;Diabetes Care,2002

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