Fructose mediated crosslinking of proteins.

D. J. Walton; John Douglas Mcpherson; B. H. Shilton

Fructose mediated crosslinking of proteins.

D. J. Walton, John Douglas Mcpherson, B. H. Shilton

Research output: Contribution to journal › Article › peer-review

Abstract

10-20% of the hexose bound to human ocular lens proteins was found to be attached to epsilon-amino groups of lysyl residues via carbon 2. It was concluded that the proteins had undergone nonenzymatic reactions with endogenous fructose. This process may be important in some mammalian tissues, owing to the high crosslinking potential of fructose.

Original language	English (US)
Pages (from-to)	163-170
Number of pages	8
Journal	Progress in Clinical and Biological Research
Volume	304
State	Published - 1989
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

Cite this

@article{97f239390d6047148cb91ccd523a97ca,

title = "Fructose mediated crosslinking of proteins.",

abstract = "10-20% of the hexose bound to human ocular lens proteins was found to be attached to epsilon-amino groups of lysyl residues via carbon 2. It was concluded that the proteins had undergone nonenzymatic reactions with endogenous fructose. This process may be important in some mammalian tissues, owing to the high crosslinking potential of fructose.",

author = "Walton, {D. J.} and Mcpherson, {John Douglas} and Shilton, {B. H.}",

year = "1989",

language = "English (US)",

volume = "304",

pages = "163--170",

journal = "Progress in Clinical and Biological Research",

issn = "0361-7742",

publisher = "John Wiley and Sons Inc.",

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T1 - Fructose mediated crosslinking of proteins.

AU - Walton, D. J.

AU - Mcpherson, John Douglas

AU - Shilton, B. H.

PY - 1989

Y1 - 1989

N2 - 10-20% of the hexose bound to human ocular lens proteins was found to be attached to epsilon-amino groups of lysyl residues via carbon 2. It was concluded that the proteins had undergone nonenzymatic reactions with endogenous fructose. This process may be important in some mammalian tissues, owing to the high crosslinking potential of fructose.

AB - 10-20% of the hexose bound to human ocular lens proteins was found to be attached to epsilon-amino groups of lysyl residues via carbon 2. It was concluded that the proteins had undergone nonenzymatic reactions with endogenous fructose. This process may be important in some mammalian tissues, owing to the high crosslinking potential of fructose.

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M3 - Article

C2 - 2506560

AN - SCOPUS:0024350270

VL - 304

SP - 163

EP - 170

JO - Progress in Clinical and Biological Research

JF - Progress in Clinical and Biological Research

SN - 0361-7742

ER -

Fructose mediated crosslinking of proteins.

Abstract

ASJC Scopus subject areas

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