A cDNA encoding spinach α-glucosidase was cloned and sequenced bythe reverse-transcription polymerase chain reaction (RT-PCR) and rapidamplification of cDNA ends (RACE) methods. The cDNA comprised 2867 bp,and included an open reading frame which encodes a polypeptide of 903amino acid residues. The calculated molecular mass of 101 kDa waslarger than those of native α-glucosidases in spinach seeds,which are 78, 78, 82, and 82 kDa by SDS-PAGE for α-glucosidase I,II, III, and IV, respectively. The deduced amino acid sequence includedthose of tryptic peptides from native enzymes. Southern blot analysissuggested that the α-glucosidase gene was a single-copy gene.These results indicate the possibility that the multiplicity ofα-glucosidase in spinach occurs via post-translationalmodification.
Plant Molecular Biology – Springer Journals
Published: Sep 29, 2004
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