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Analysis of cell wall proteins, either by sodium dodecyl sulphate\u2013polyacrylamide gel electrophoresis of extractable mannoproteins or by immunolocalization, revealed an accumulation of a protein with Mr 37 kDa (p37), upon flocculation. Immunological studies confirmed the homology of this protein with the glycolytic enzyme glyceraldehyde\u20103\u2010phosphate dehydrogenase (GAPDH). When mRNA isolated from cells growing at 40\u00b0C was translated <jats:italic>in vitro<\/jats:italic>, a 35 kDa newly labelled protein was synthesized and immunoprecipitation assays showed that this protein is recognized by p37\u2010antiserum, suggesting that the 35 kDa polypeptide might be an unglycosylated precursor form of p37. The results indicated that the presence of this cell wall mannoprotein closely related to GAPDH is dependent on the growth temperature, suggesting its role as adhesin.<\/jats:p>","DOI":"10.1002\/yea.320090806","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T23:44:41Z","timestamp":1117323881000},"page":"859-866","source":"Crossref","is-referenced-by-count":23,"title":["Flocculation of <i>Kluyveromyces marxianus<\/i> is induced by a temperature upshift"],"prefix":"10.1002","volume":"9","author":[{"given":"P. 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