Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Jennifer M. Ye"'
Publikováno v:
Pharmaceutical Research. 15:1808-1815
Purpose. To study the effects of recombinant human protein disulfide isomerase (rhPDI) concentration, reduced glutathione:oxidized glutathione ratio (GSH:GSSG) and temperature on the efficiency of oxidative folding of a model protein, recombinant hum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::681c146b537596c27b9cfccc34fca2f2
https://doi.org/10.1023/a:1011941603339
https://doi.org/10.1023/a:1011941603339
Publikováno v:
Journal of Pharmaceutical Sciences. 85:695-699
Antiflammin 2 (HDMNKVLDL, AF2) is a synthetic peptide derived from the region of highest sequence similarity of lipocortin I and uteroglobin, and is a potent antiinflammatory agent without any known side effects of corticosteroids. The antiinflammato
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cb466260300d02df161224902e52e75
https://doi.org/10.1021/js960006f
https://doi.org/10.1021/js960006f
Publikováno v:
Biochemical and Biophysical Research Communications. 223:153-159
Protein disulfide isomerase has broad specificity in the catalysis of the formation and rearrangement of native disulfide bonds in proteins. This enzyme has two independent thioredoxin-like active sites (-CGHC-) and a peptide binding site. However, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8361f2036e548d8806260bfe772d5af
https://doi.org/10.1006/bbrc.1996.0861
https://doi.org/10.1006/bbrc.1996.0861
Autor:
Jennifer M. Ye, Janet L. Wolfe
Publikováno v:
Pharmaceutical Research. 13:250-255
Purpose. To study the oxidation of the methionine residue of antiflammin 2 (HDMNKVLDL, AF2) as a function of pH, buffer concentration, ionic strength, and temperature using different concentrations of hydrogen peroxide and to determine the accessibil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85fb3dbdba643129c0b40e1e2b6de851
https://doi.org/10.1023/a:1016095131836
https://doi.org/10.1023/a:1016095131836