Abstract
Rat brain homogenate was incubated with various concentrations of ascorbate in a Tris-HCl buffer. Thiobarbituric acid-reactive substances (TBARS) were measured and 3H-QNB (quinuclidinyl benzilate) binding was also assayed on the same homogenate. Good parallelism between TBARS formation and loss of 3H-QNB binding activity confirmed that loss of 3H-QNB binding resulted from ascorbate-induced lipid peroxidation. However, neither formation of TBARS nor loss of 3H-QNB binding occurred in phosphate buffer or in the Tris-HCl system in the presence of metal-chelating reagents. This indicates that phosphate addition prevents the ascorbate effects due to complete chelation of intrinsic metal ions.
| Original language | English |
|---|---|
| Pages (from-to) | 341-348 |
| Number of pages | 8 |
| Journal | Biochemistry International |
| Volume | 11 |
| Issue number | 3 |
| Publication status | Published - 1985 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Ascorbate induced lipid peroxidation results in loss of receptor binding in Tris, but not in phosphate, buffer. Implications for the involvement of metal ions. / Abe, Koji; Kogure, K.; Arai, H.; Nakano, M.
In: Biochemistry International, Vol. 11, No. 3, 1985, p. 341-348.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ascorbate induced lipid peroxidation results in loss of receptor binding in Tris, but not in phosphate, buffer. Implications for the involvement of metal ions
AU - Abe, Koji
AU - Kogure, K.
AU - Arai, H.
AU - Nakano, M.
PY - 1985
Y1 - 1985
N2 - Rat brain homogenate was incubated with various concentrations of ascorbate in a Tris-HCl buffer. Thiobarbituric acid-reactive substances (TBARS) were measured and 3H-QNB (quinuclidinyl benzilate) binding was also assayed on the same homogenate. Good parallelism between TBARS formation and loss of 3H-QNB binding activity confirmed that loss of 3H-QNB binding resulted from ascorbate-induced lipid peroxidation. However, neither formation of TBARS nor loss of 3H-QNB binding occurred in phosphate buffer or in the Tris-HCl system in the presence of metal-chelating reagents. This indicates that phosphate addition prevents the ascorbate effects due to complete chelation of intrinsic metal ions.
AB - Rat brain homogenate was incubated with various concentrations of ascorbate in a Tris-HCl buffer. Thiobarbituric acid-reactive substances (TBARS) were measured and 3H-QNB (quinuclidinyl benzilate) binding was also assayed on the same homogenate. Good parallelism between TBARS formation and loss of 3H-QNB binding activity confirmed that loss of 3H-QNB binding resulted from ascorbate-induced lipid peroxidation. However, neither formation of TBARS nor loss of 3H-QNB binding occurred in phosphate buffer or in the Tris-HCl system in the presence of metal-chelating reagents. This indicates that phosphate addition prevents the ascorbate effects due to complete chelation of intrinsic metal ions.
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UR - http://www.scopus.com/inward/citedby.url?scp=0022416541&partnerID=8YFLogxK
M3 - Article
VL - 11
SP - 341
EP - 348
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 3
ER -