Premium
Degradation of the Large Subunit of Ribulose‐1, 5‐Bisphosphate Carboxylase/Oxygenase in Wheat Leaves
Author(s) -
ZHANG LieFeng,
RUI Qi,
XU LangLai
Publication year - 2005
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2005.00011.x
Subject(s) - rubisco , ribulose 1,5 bisphosphate , oxygenase , biochemistry , ribulose , enzyme , pyruvate carboxylase , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , gel electrophoresis , chloroplast , chemistry , protein subunit , pepstatin , biology , protease , gene
The degradation of the large subunit (LSU) of ribulose‐1, 5–bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) in wheat ( Triticum aestivum L. cv. Yangmai 158) leaves was investigated. A 50 kDa fragment, a portion of the LSU of Rubisco, was detected by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and immunoblotting with antibody against tobacco Rubisco in crude enzyme extract of young wheat leaves. The appearance of the 50 kDa fragment was most obvious at 30–35 °C and pH 5.5. The LSU and its 50 kDa fragment both existed when the crude enzyme extract was incubated for 60 min. The amount of LSU decreased with incubation time from 0 to 3 h in crude enzyme extract. However, the 50 kDa fragment could not be found any pH from 4.5 to 8.5 in chloroplast lysates of young wheat leaves. In addition, through treatment with various inhibitors, reactions were inhibited by cysteine proteinase inhibitor E‐64 or leupeptin. ( Managing editor: Ping HE)