A simple preparation method for apoaspartate aminotransferase from Escherichia coli B, and its application for the assay of pyridoxal and pyridoxamine 5'-phosphate.

Abstract:

:A simple and rapid preparation method for apoaspartate aminotransferase from Escherichia coli B was developed. A crude extract of the bacterial cells was treated batchwise with DEAE-cellulose. The enzyme fraction obtained was then applied to a pyridoxamine-Sepharose column. Apoaspartate aminotransferase was eluted with 50 mM potassium phosphate buffer (pH 7.0), and found to be electrophoretically homogeneous. The apoenzyme preparation thus obtained showed very low holoenzyme activity (only 0.4% of the activity seen in the fully saturated condition with pyridoxal 5'-phosphate) and was successfully used for assaying pyridoxal and pyridoxamine 5'-phosphate.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Yagi T,Kirino J,Yamamoto S,Nozaki M

doi

10.1093/oxfordjournals.jbchem.a135371

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

921-6

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

98

pub_type

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