Rapid purification of malate synthase from cotyledons of Brassica napus L.

Abstract:

:A rapid and efficient method for the purification of malate synthase, an enzyme uniquely confined to glyoxysomes, from cotyledons of Brassica napus L. has been developed. The two step purification procedure is based on the consequent utilization of the tendency of malate synthase to form high molecular weight aggregates. Malate synthase was purified 75-fold to apparent homogeneity with a specific activity of 180 nkat/mg protein. The estimated molecular weight of malate synthase subunits was 63 kDa. Polyclonal antibodies raised against malate synthase in rabbits detect on Western blots only one single polypeptide with an identical molecular weight.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hoppe A,Theimer RR

doi

10.1016/0014-5793(95)01114-t

subject

Has Abstract

pub_date

1995-10-30 00:00:00

pages

225-7

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01114-T

journal_volume

374

pub_type

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