[Hypocrellin A-sensitized photodamage on erythrocyte membrane protein and phospholipid].
In this paper, using human erythrocyte membrane, the photodamage of Hypocrellin A to membrane protein and phospholipid was studied by measuring the lipid peroxidation, the damage of phospholipid, the change of protein secondary structure, the endogenous fluorescence change and SDS-polyacrylamide gel electrophoresis analysis. These results showed that illumination of erythrocyte membrane in presence of Hypocrellin A can cause lipid peroxidation producing fluorescence adduct and MDA, decomposing in phospholipid composition in which PE and PS were more sensitive than others. Meanwhile, the secondary structure of membrane protein was destroyed and endogenous fluorescence decreased. The photodamage on phospholipid and spectrin occurred more seriously in the case they were embedded in membrane than they were in isolated form. So we suggest that they are interactions existing between proteins and phospholipids to enhance the damage on protein and phospholipid during the HA-sensitized photodamage on membrane.
Du
J A
JA
Institute of Biophysics, Academia Sinica, Beijing.
Qin
J F
JF
Zhang
X Z
XZ
Cheng
L S
LS
D001551:Benz(a)Anthracenes / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects*; D006801:Humans; D008027:Light; D015227:Lipid Peroxidation / Q000187:drug effects; D008565:Membrane Proteins / Q000187:drug effects*; D010569:Perylene / Q000031:analogs & derivatives / Q000494:pharmacology*; D019800:Phenol; D010743:Phospholipids; D011809:Quinones / Q000494:pharmacology*; D011838:Radiation-Sensitizing Agents; D013049:Spectrin / Q000187:drug effects
D001551:Benz(a)Anthracenes; D008565:Membrane Proteins; D010743:Phospholipids; D011809:Quinones; D011838:Radiation-Sensitizing Agents; D013049:Spectrin; D019800:Phenol; D010569:Perylene; C048388:hypocrellin A