Abstract
A vacuolar processing enzyme was detected in soybean protein bodies. A 39-kDa immunoreactive polypeptide obtained by chromatography on a hydroxyapatite column processed both a decapeptide substrate and proproteins. A cDNA was isolated for a 55-kDa protein with 71% identity to the castor bean vacuolar processing enzyme.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Chromatography
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Cysteine Endopeptidases / chemistry
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Cysteine Endopeptidases / isolation & purification
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Cysteine Endopeptidases / metabolism*
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DNA Primers
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DNA, Complementary / isolation & purification
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Durapatite
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Glycine max / enzymology*
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Molecular Sequence Data
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Molecular Weight
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Plants, Toxic
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Protein Precursors / metabolism*
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Ricinus communis / enzymology
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Schistosoma / enzymology
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Sequence Homology, Amino Acid
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Substrate Specificity
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Vacuoles / enzymology
Substances
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DNA Primers
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DNA, Complementary
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Protein Precursors
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Durapatite
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Cysteine Endopeptidases
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vacuolar processing enzyme
Associated data
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GENBANK/D28876
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PIR/S31908