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Identification and characterization of a rice cysteine endopeptidase that digests glutelin.
- Source :
- European Journal of Biochemistry; 7/15/96, Vol. 239 Issue 2, p310-316, 7p
- Publication Year :
- 1996
-
Abstract
- Little or no endopeptidase activity was detected in extracts from storage organs of dark-grown rice seeds until day 6 of post-imbibition, and the activity expressed per seed increased notably after day 9, reached a maximum on day 18, then decreased. Two major endopeptidases, REP-1 and REP-2, were present in the 40-75% saturated ammonium sulfate fraction from day-9 germinated seeds, and could be separated by hydrophobic column chromatography. REP-1 was further purified to a single polypeptide of 36 kDa. REP-1 digested in vitro both the acidic and basic subunits of rice glutelin, the major seed storage protein of rice. Determination of the N-terminal amino acid sequence and experiments with protease inhibitors indicated that REP-1 is a cysteme endopeptidase. Tile nucleotide sequence of a full-length REP-1 cDNA was determined by a combination of screening of cDNA libraries from rice seeds and the 5′ rapid amplification of cDNA ends technique. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 239
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13055322
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1996.0310u.x