Publication:
LENS GLUTATHIONE, LENS PROTEIN GLYCATION AND ELECTROPHORETIC PATTERNS OF LENS PROTEINS IN STZ INDUCED DIABETIC RATS

dc.contributor.authorsYARAT, A; UGUZ, Z; USTUNEL, A; EMEKLI, N
dc.date.accessioned2022-03-12T16:57:11Z
dc.date.accessioned2026-01-10T17:32:49Z
dc.date.available2022-03-12T16:57:11Z
dc.date.issued1995
dc.description.abstractAs diabetes is a very complex disease, with the pathological symptoms varying with age, diabetic type and means of control, it still warrants many in vivo and in vitro studies. During hyperglycaemia, increases in the sorbitol pathway, nonenzymatic glycosylation of lens proteins and damage to antioxidant systems have been reported to cause opacification of the lens leading to cataract formation. In this study, intracapsular extracts of lenses from STZ induced diabetic female rats were examined. Total protein, glutathione and nonenzymatic glycosylation were determined by the Lowry, Ellman reagent and thiobarbituric acid methods respectively. Laemmli protein electrophoresis was also carried out on the lens homogenates. After a period of as short as 5 weeks, a decrease in lens glutathione, and an increase in nonenzymatic glycosylation of lens proteins were found. The electrophoresis showed an increase in proteins of high molecular weight.
dc.identifier.doi10.1007/BF00731256
dc.identifier.issn0282-0080
dc.identifier.pubmed8595251
dc.identifier.urihttps://hdl.handle.net/11424/226895
dc.identifier.wosWOS:A1995RZ73100003
dc.language.isoeng
dc.publisherCHAPMAN HALL LTD
dc.relation.ispartofGLYCOCONJUGATE JOURNAL
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectLENS
dc.subjectDIABETES
dc.subjectGLUTATHIONE
dc.subjectNONENZYMATIC GLYCOSYLATION
dc.subjectELECTROPHORESIS
dc.subjectALDOSE REDUCTASE
dc.subjectCATARACTOGENESIS
dc.subjectCRYSTALLINS
dc.subjectGLUCOSE
dc.subjectGLYCOSYLATION
dc.subjectINVITRO
dc.titleLENS GLUTATHIONE, LENS PROTEIN GLYCATION AND ELECTROPHORETIC PATTERNS OF LENS PROTEINS IN STZ INDUCED DIABETIC RATS
dc.typearticle
dspace.entity.typePublication
oaire.citation.endPage626
oaire.citation.issue5
oaire.citation.startPage622
oaire.citation.titleGLYCOCONJUGATE JOURNAL
oaire.citation.volume12

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