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- W2078442626 abstract "A cellulase (β(1:4)4-glucan hydrolase) has been purified 700-fold by cellulose affinity chromatography from anthers of Lathyrus odoratus L. Two forms are present. The major species has a molecular weight of 49 kDa and a pI value of 8.0; the minor a molecular weight of 51 kDa and a pI value of 7.8. Both proteins are recognized by antibodies raised against the ethylene/IAA regulated bean (Phaseolus vulgaris L.) abscission zone cellulase which has a more basic pI value and some unique antigenic determinants. Ethylene induced Lathyrus flower bud abscission zones contain two forms of cellulase apparently identical to those in the anthers. The possible role of cellulase in the development of anthers is discussed." @default.
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- W2078442626 date "1990-01-01" @default.
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- W2078442626 title "The purification of an anther cellulase (β(1:4)4-glucan hydrolase) from Lathyrus odoratus L. and its relationship to the similar enzyme found in abscission zones" @default.
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- W2078442626 doi "https://doi.org/10.1016/0168-9452(90)90240-o" @default.
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