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GrainGenes Reference Report: JCS-30-227

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Reference
JCS-30-227
Title
Occurrence and stabilities of oat trypsin and chymotrypsin inhibitors
Journal
Journal of Cell Science
Year
1999
Volume
30
Pages
227-235
Author
Mikola M
Mikkonen A
Abstract
Nine chymotrypsin and four trypsin inhibitors have been extracted and separated from ungerminated oat grains The inhibitors fell into two groups, based on their heat and pH stabilities Members of the most abundant group are labile and are inactivated at 80 degrees C or at pHs of 3.3 or lower Members of the second group are stable and are resistant to boiling for 30 min On germination, the labile inhibitors are inactivated after 2 days and the stable chymotrypsin inhibitors after 3 days Most of the labile inhibitors from ungerminated grain are destroyed when incubated at 20 degrees C for 20 h but addition of PMSF, a serine protease inhibitor, prevented their inactivation. Labile inhibitors in extracts of ungerminated oats are inactivated on incubation with an extract prepared from germinated oats, but not in the presence of PMSF. Most oat chymotrypsin and trypsin inhibitors are heat labile and pH sensitive. These inhibitors are apparently inactivated by serine proteinase(s) already present in ungerminated grain.
Keyword
avena sativa
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