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Phosphoglycolate phosphatase: purification and preparation of antibodies

✍ Scribed by Faith C. Belanger; William L. Ogren

Publisher
Springer
Year
1987
Tongue
English
Weight
803 KB
Volume
14
Category
Article
ISSN
0166-8595

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✦ Synopsis

Phosphoglycolate phosphatase was partially purified from leaves of Nicotiana rustica using ion exchange and chromatofocusing columns. The native molecular weight of the enzyme was determined to be about 58 kD from Ferguson plots, with a subunit size of about 32 kD. The native enzyme is thus likely to be a dimer. A polyclonal antibody prepared against the LDS denatured enzyme cross reacted with proteins from Nicotiana tabacum, Glycine max, Spinacea oleracea and Arabidopsis thaniana. There was little or no reaction with an Arabidopsis mutant lacking phosphoglycolate ph0sphatase activity, indicating a much reduced level of phosphoglycolate phosphatase protein in the mutant.

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