Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1988-7-15
|
pubmed:abstractText |
Incubation of carbohydrate-free human serum albumin (HSA) with fructose in an aqueous buffer at pH 7.4 resulted in glycation of epsilon-amino groups of lysyl residues. A recently developed procedure, involving analysis of hexitol amino acids by high-performance liquid chromatography of phenylthiocarbamyl derivatives, was used to show that 85% of the bound hexose was attached to protein via carbon 2 (C-2). The remainder was attached to protein via carbon 1 (C-1). When incubations were conducted with glucose under identical conditions, all the hexose was attached via C-1. Examination of human ocular lens proteins showed that the majority of the covalently bound hexose was connected to epsilon-amino groups of lysyl residues via C-1; this was attributed mainly to nonenzymatic glucosylation in vivo, which has already been documented. A significant proportion (10-20%) of the bound hexose was connected via C-2. In view of the HSA-hexose incubation results (above), this indicated that the lens proteins had reacted with endogenous fructose; i.e., they had undergone nonenzymatic fructosylation in vivo. The model protein bovine pancreatic ribonuclease A reacted with fructose and glucose at similar rates under physiological conditions. However, covalent, non-disulfide cross-linking, which could be inhibited by D-penicillamine, was induced 10 times more rapidly by fructose than by glucose. It is postulated that some of the protein cross-linking that occurs in vivo is fructose-induced. The possible significance of these processes in diabetic subjects is discussed.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Crystallins,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillamine,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
22
|
pubmed:volume |
27
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1901-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3132203-Cross-Linking Reagents,
pubmed-meshheading:3132203-Crystallins,
pubmed-meshheading:3132203-Fructose,
pubmed-meshheading:3132203-Glycosylation,
pubmed-meshheading:3132203-Humans,
pubmed-meshheading:3132203-Lysine,
pubmed-meshheading:3132203-Magnetic Resonance Spectroscopy,
pubmed-meshheading:3132203-Mass Spectrometry,
pubmed-meshheading:3132203-Penicillamine,
pubmed-meshheading:3132203-Serum Albumin,
pubmed-meshheading:3132203-Spectrometry, Fluorescence
|
pubmed:year |
1988
|
pubmed:articleTitle |
Role of fructose in glycation and cross-linking of proteins.
|
pubmed:affiliation |
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|