Isolation of Coconut Storage Proteins by Polyacrylamide-Gel Electrophoresis

dc.contributor.authorRobert W. Wallace
dc.contributor.authorJulius W. Dieckert
dc.date.accessioned2014-09-03T04:39:42Z
dc.date.available2014-09-03T04:39:42Z
dc.date.issued2007
dc.description.abstractBy combining sodium dodecyl sulfate (SDS)-gel electrophoresis with a new chilling technique for visualization of protein-SDS complexes in polyacrylamide gels, a process has been developed which will permit the isolation of milligram quantities of pure polypeptides. Using this technique, we have isolated two molecular weight classes of polypeptides from coconut storage globulins and do'- mined the amino acid composition of each. When the two amino acid compos tions were summed on a molar basis, the result agreed reasonably well with the amino acid composition of the starting material with the exception of cystine. Apparently, some contaminant from the polyacrylamide caused its destruction to be accelerated during hydrolysis.en_US
dc.identifier.urihttp://hdl.handle.net/123456789/5299
dc.language.isoenen_US
dc.titleIsolation of Coconut Storage Proteins by Polyacrylamide-Gel Electrophoresisen_US
dc.typeArticleen_US

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