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 Lettjournal_title
FEBS lettersauthors
Hoppe A,Theimer RRdoi
10.1016/0014-5793(95)01114-tsubject
Has Abstractpub_date
1995-10-30 00:00:00pages
225-7issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(95)01114-Tjournal_volume
374pub_type
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