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PLANT PHYSIOLOGY , Vol 106, Issue 2 521-528, Copyright © 1994 by American Society of Plant Biologists
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METABOLISM AND ENZYMOLOGY |
Apple [beta]-Galactosidase (Activity against Cell Wall Polysaccharides and Characterization of a Related cDNA Clone)
G. S. Ross, T. Wegrzyn, E. A. MacRae and R. J. Redgwell
The Horticulture and Food Research Institute of New Zealand Ltd., Mt. Albert Research Centre, Private Bag 92 169, Auckland, New Zealand
A [beta]-galactosidase was purified from cortical tissue of ripe apples
(Malus domestica Borkh. cv Granny Smith) using a procedure involving
affinity chromatography on lactosyl-Sepharose. Sodium dodecyl
sulfate-polyacrylamide gel electrophoresis indicated that two polypeptides
of 44 and 32 kD were present in the fraction that showed activity against
the synthetic substrate p-nitrophenol-[beta]-D-galactopyranoside. The
enzyme preparation was incubated with polysaccharide extracts from apple
cell walls containing [beta]-(1->4)-linked galactans, and products of
digestion were analyzed by gas chromatography. Small amounts of monomeric
galactose were released during incubation, showing that the enzyme was
active against native substrates. Amino acid sequence information was
obtained from the purified protein, and this showed high homology with the
anticipated polypeptide coded by the ethylene-regulated SR12 gene in
carnation (K.G. Raghothama, K.A. Lawton, P.B. Goldborough, W.R. Woodson
[1991] Plant Mol Biol 17: 61-71) and a harvest-related pTIP31 cDNA from
asparagus (G. King, personal communication). Using the asparagus cDNA clone
as a probe, an apple homolog (pABG1) was isolated. This clone contains a
2637-bp insert, including an open reading frame that codes for a
polypeptide of 731 amino acids. Cleavage of an N-terminal signal sequence
would leave a predicted polypeptide of 78.5 kD. Genomic DNA analysis and
the isolation of other homologous apple clones suggest that pABG1
represents one member of an apple [beta]-galactosidase gene family.
Northern analysis during fruit development and ripening showed accumulation
of pABG1-homologous RNA during fruit ripening. Enzyme activity as measured
in crude extracts increased during fruit development to a level that was
maintained during ripening.
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