[The study on hypocrellin A-sensitized photoinactivation of enzymes of human erythrocyte membranes].
Hypocrellin A (HA)-sensitized photoinactivation of enzymes in human erythrocyte membrane, including AchE, GPDH, Na(+)-K+ ATPase, Ca2(+)-Mg2+ ATPase were studied in this paper. The sensitivity of these four enzymes inactivated by HA and light are as following order: Ca2(+)-Mg2+ ATPase greater than Na(+)-K+ ATPase greater than GPDH greater than AchE. The relationship among ATPase inactivation, sulfhydryl photoinactivation and lipid peroxidation was also investigated. Results show that SH group photooxidation probably is one of the major reasons of enzyme inactivation whereas lipid peroxidation has little effect. The isolated GPDH was less sensitive than that membrane-bound, GSH, NAD acted protectively on GPDH and ATPase respectively. The evidence of electrophoresis and protein intrinsic fluorescence showed that protein structure did not change significantly even though most activity had lost in case of GPDH.
Sun
J S
JS
Cheng
L S
LS
Qin
J F
JF
D000110:Acetylcholinesterase / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006801:Humans; D010569:Perylene / Q000031:analogs & derivatives*; D019800:Phenol; D011809:Quinones / Q000494:pharmacology*; D011838:Radiation-Sensitizing Agents
D011809:Quinones; D011838:Radiation-Sensitizing Agents; D019800:Phenol; D010569:Perylene; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D000110:Acetylcholinesterase; D000251:Adenosine Triphosphatases; C048388:hypocrellin A