1987
DOI: 10.1016/0009-3084(87)90054-5
|View full text |Cite
|
Sign up to set email alerts
|

Involvement of lipid oxidation products in the formation of fluorescent and cross-linked proteins

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

6
115
0
1

Year Published

1994
1994
2015
2015

Publication Types

Select...
6
3

Relationship

1
8

Authors

Journals

citations
Cited by 165 publications
(122 citation statements)
references
References 130 publications
6
115
0
1
Order By: Relevance
“…6A), suggesting that the fluorescence is due to chromophores of another structure. 32) From these findings, it seems that the discrepancy observed between HNE-and MDA-modified synaptosomes may reflect the difference in action mechanisms of these aldehydic compounds on the synaptosomal Na ϩ -K ϩ -ATPase described above, although the exact mechanisms are unclear at present.…”
Section: Discussionmentioning
confidence: 87%
“…6A), suggesting that the fluorescence is due to chromophores of another structure. 32) From these findings, it seems that the discrepancy observed between HNE-and MDA-modified synaptosomes may reflect the difference in action mechanisms of these aldehydic compounds on the synaptosomal Na ϩ -K ϩ -ATPase described above, although the exact mechanisms are unclear at present.…”
Section: Discussionmentioning
confidence: 87%
“…Therefore, three different prediction models were constructed for each of the three maturation indices: maturation time, proteolysis index and total free amino acids. Table 1 Multiple chemical components are known to fluoresce in this wavelength range such as oxidized lipids (Dillard and Tappel, 1971), Maillard reaction products (Birlouez-Aragon et al, 1998;Birlouez-Aragon et al, 2002;Morales et al, 1996;Morales and van Boekel, 1998;Schamberger and Labuza, 2006) and Schiff bases formed between oxidation products and amino groups (Kikugawa and Beppu, 1987). Maillard products are most often linked to the heating process of dairy products, but are known to increase with maturation time (Corzo et al, 2000) and have also been used as an indicator of cheese ripening (Pellegrino et al, 1997).…”
Section: Resultsmentioning
confidence: 99%
“…2). [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] However, characteristics of the fluorescence due to MA were not identical with those due to peroxidized lipids. [16][17][18][19] In contrast, monofunctional aldehydes produced fluorescence at 430-440 nm, whose characteristics were close to those of peroxidized lipids.…”
Section: Damage To Proteins Through Lipid Peroxidationmentioning
confidence: 96%
“…3. 15,25) Blue fluorescent substances extracted from rat tissues by sodium dodecylsulfate (SDS) and purified by gel filtration showed characteristics similar to those of the fluorescence from the reaction between amines with peroxidized lipids and monofunctional aldehydes. 18,26,27) Hence, it was concluded that protein damage due to lipid peroxidation was caused mainly by monofunctional aldehydes and little by free MA.…”
Section: Damage To Proteins Through Lipid Peroxidationmentioning
confidence: 98%