Open AccessPurification and some properties of malate synthase from the methylotrophic yeast Hansenula polymorpha
Author(s) -
Bruinenberg P.G.,
Blaauw M.,
Veenhuis M.,
Ab G.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03543.x
Subject(s) - malate synthase , glyoxylate cycle , biochemistry , malate dehydrogenase , enzyme , biology , polyacrylamide gel electrophoresis , yeast , atp synthase , molecular mass , size exclusion chromatography , gel electrophoresis , microbiology and biotechnology , chemistry , isocitrate lyase
Malate synthase, one of the key enzymes in the glyoxylate cycle, was purified 122‐fold to homogeneity from ethanol‐grown Hansenula polymorpha . SDS‐polyacrylamide gel electrophoresis showed that the enzyme has a subunit size of 62 000 daltons. The molecular mass of native malate synthase was determined to be 250 000 daltons by gel filtration, indicating that the enzyme is a tetramer. Cell fractionation studies and immunogold staining, carried out on ultrathin sections of ethanol‐grown H. polymorpha , using malate synthase‐specific antibodies, showed that malate synthase was localized in the matrix of peroxisomes.