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pubmed-article:2505756pubmed:abstractTextMaltase activity (EC 3.2.1.20) was solubilized from rabbit kidney brush-border membrane by using 1.0% Triton X-100 and purified 230-fold with an overall recovery of 30%. The purification procedure makes use of heat precipitation, chromatography on DE-52 DEAE-cellulose and gel filtration on Sephacryl S-300. Rabbit kidney brush border exhibited glucoamylase activity with a maltase/glucoamylase ratio of 1.5:1 to 2.0:1. During purification the maltase and glucoamylase activities behaved identically. The Mr of the complex is 590,000, and it appears to be composed of eight identical subunits linked by disulphide bridges.lld:pubmed
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pubmed-article:2505756pubmed:authorpubmed-author:SivakamiSSlld:pubmed
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pubmed-article:2505756pubmed:year1989lld:pubmed
pubmed-article:2505756pubmed:articleTitleNeutral maltase/glucoamylase from rabbit renal cortex.lld:pubmed
pubmed-article:2505756pubmed:affiliationDepartment of Life Sciences, University of Bombay, India.lld:pubmed
pubmed-article:2505756pubmed:publicationTypeJournal Articlelld:pubmed
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