Dissociation-recombination of sunflower seed acid phosphatase

Formal genetic studies of sunflower (Helianthus annuus) seed acid phosphatase (ACP, E.C. 3.1.3.2) had suggested that the functional enzyme consists of two polypeptide subunits. The dimeric quaternary structure was demonstrated by dissociation-recombination procedures. Dissociation of electrophoretic...

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Bibliographic Details
Published inBiochemical genetics Vol. 15; no. 9-10; p. 897
Main Authors Torres, A M, Diedenhofen, U
Format Journal Article
LanguageEnglish
Published United States 01.10.1977
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Summary:Formal genetic studies of sunflower (Helianthus annuus) seed acid phosphatase (ACP, E.C. 3.1.3.2) had suggested that the functional enzyme consists of two polypeptide subunits. The dimeric quaternary structure was demonstrated by dissociation-recombination procedures. Dissociation of electrophoretically distinct homodimers was effected upon freezing of extracts in a pH 8-9 buffer containing 1 M NaCl and 0.1 M 2-mercaptoethanol. Reassociation, as indicated by the formation of the hybrid isozyme, occurred during 12 hr dialysis against a pH 7.0 buffer.
ISSN:0006-2928
DOI:10.1007/BF00483985