These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Glycated Cu,Zn-superoxide dismutase in rat lenses: evidence for the presence of fragmentation in vivo. Author: Takata I, Kawamura N, Myint T, Miyazawa N, Suzuki K, Maruyama N, Mino M, Taniguchi N. Journal: Biochem Biophys Res Commun; 1996 Feb 06; 219(1):243-8. PubMed ID: 8619815. Abstract: Cu,Zn-superoxide dismutase (Cu,Zn-SOD) exists in tissues of rats as both glycated and non-glycated forms when separated by boronate acid column chromatography. Glycated Cu.Zn-SOD is most abundant in rat lenses compared to other tissues. In normal rats lens levels of glycated Cu.Zn-SOD showed a gradual increase with age, whereas in diabetic rats substantial increases were observed. Immunoblotting analyses, using anti-hexitol lysine IgG, indicated that glycated Cu.Zn-SOD contains Amadori products. Moreover, Cu.Zn-SOD in lenses was site-specifically fragmented probably because of glycation. This the first report of a fragmented protein, such as Cu,Zn-SOD, occurring in vivo.[Abstract] [Full Text] [Related] [New Search]