Chemical and Pharmaceutical Bulletin
Online ISSN : 1347-5223
Print ISSN : 0009-2363
ISSN-L : 0009-2363
Studies on the Active Site of Papain. VI. Chemical Modification of Tryptophan Residues by N-Bromosuccinimide
MASUMI SAKANEHARUO KANAZAWAAKIRA OHARA
Author information
JOURNAL FREE ACCESS

1975 Volume 23 Issue 8 Pages 1741-1744

Details
Abstract
1) The present research has been planed to demonstrate the importance of tryptophan residues on enzyme activity of papain by means of NBS oxidation. 2) About 2 tryptophan residues were oxidized and the first oxidizable tryptophan was important for enzyme activity. 3) The relationship between tryptophan oxidation and enzyme activity for acetylpapain and mercuripapain are quite similar to that for papain. 4) About 1 tryptophan and 3 tyrosine residues in papain were modified by NBS oxidation. However, only 1 tryptophan residue and no tyrosine residue in acetylpapain were oxidized at complete inactivation. 5) The acetylation of tyrosine in papain prevented the tyrosine from oxidizing by NBS. 6) SH group and histidine residues in papain were not affected by NBS oxidation. 7) These results indicate that the modification of a tryptophan residue by NBS oxidation causes loss of the enzyme activity.
Content from these authors
© The Pharmaceutical Society of Japan
Previous article Next article
feedback
Top