The purification and characterization of methylmalonyl CoA mutase from bovine brain
Methylmalonyl CoA mutase has been purified over 2300-fold from bovine brain using fractional precipitation, ion exchange resins, and gel filtration procedures. The crude extract had an equal mixture of mutase in the halo- and apoenzyme form. After the final purification step the ratio had changed to...
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| Format: | Others |
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BYU ScholarsArchive
1974
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| Online Access: | https://scholarsarchive.byu.edu/etd/8305 https://scholarsarchive.byu.edu/cgi/viewcontent.cgi?article=9305&context=etd |