Abstract:
:Glycophorin from human red blood cells was exposed to ozone in aqueous solution. Amino acid analysis of glycophorin exposed to a 10-fold molar excess of ozone showed that the only residue affected was methionine. Both methionine residues of the protein were oxidized to methionine sulfoxide. Exposure of the oxidized protein to cyanogen bromide caused no cleavage of the polypeptide chain. Glycophorin was incorporated into unilamellar lipid vesicles made from phosphatidylcholine. The protein containing vesicles were exposed to ozone in a 10-fold molar excess to the glycophorin. Gas chromatography of the methyl esters showed negligible change in the fatty acid composition. Amino acid analysis of the ozone-treated protein showed the oxidation of only one methionine residue per polypeptide chain to methionine sulfoxide. Ghosts of human erythrocytes were exposed to ozone. Cyanogen bromide treatment of the oxidized glycophorin yielded fragments showing that the only methionine residue oxidized by ozone was residue 8. These results indicate that in this membrane model (a) amino acid is more susceptible to ozone than is the lipid, and (b) amino acids external to the membrane are more susceptible than those in the polypeptide chain spanning the membrane.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Banerjee SK,Mudd JBdoi
10.1016/0003-9861(92)90491-esubject
Has Abstractpub_date
1992-05-15 00:00:00pages
84-9issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(92)90491-Ejournal_volume
295pub_type
杂志文章abstract::The fundamental improvement of muscle ischemia requires the re-establishment of sufficient vessel network. Despite many kinds of drugs have been used for ischemia, effective angiogenic drug is very limited. Here, we reported the identification and isolation of a potent angiogenic fraction (angio-T) from Geum japonicum...
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