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Glycation sites of human plasma proteins are affected to different extents by hyperglycemic conditio...

Glycation sites of human plasma proteins are affected to different extents by hyperglycemic conditio...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1808082892

Glycation sites of human plasma proteins are affected to different extents by hyperglycemic conditions in type 2 diabetes mellitus

About this item

Full title

Glycation sites of human plasma proteins are affected to different extents by hyperglycemic conditions in type 2 diabetes mellitus

Publisher

Berlin/Heidelberg: Springer Berlin Heidelberg

Journal title

Analytical and bioanalytical chemistry, 2014-09, Vol.406 (24), p.5755-5763

Language

English

Formats

Publication information

Publisher

Berlin/Heidelberg: Springer Berlin Heidelberg

More information

Scope and Contents

Contents

Glucose can modify proteins in human blood, forming early glycation products (e.g., Amadori compounds), which can slowly degrade to advanced glycation endproducts (AGEs). AGEs contribute significantly to complications of diabetes mellitus and, thus, represent markers of advanced disease stages. They are, however, currently unsuitable for early diag...

Alternative Titles

Full title

Glycation sites of human plasma proteins are affected to different extents by hyperglycemic conditions in type 2 diabetes mellitus

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1808082892

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1808082892

Other Identifiers

ISSN

1618-2642

E-ISSN

1618-2650

DOI

10.1007/s00216-014-8018-y

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