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Purification of sexual agglutination factor from the yeastHansenula wingeiby chromatography and gradient sedimentation

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
111
Issue
1
Identifiers
DOI: 10.1016/0003-9861(65)90337-1
Disciplines
  • Biology

Abstract

Abstract The agglutination factor from mating type 5 of Hansenula wingei was fractionated by various techniques. The factor was heterogeneous in chromatography on phospho-cellulose and notably broad in its sedimentation distribution diagram. Highly active fractions could be obtained either from chromatography on phospho-cellulose or from fractions sedimenting at rates greater than 100 Svedbergs. The most active fractions had particle weights greater than 10 8, and only a few of these particles per cell were required to agglutinate the opposite mating type. The agglutinating factor appears to be a protein-mannan complex.

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