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. 1978 Apr;61(4):581–584. doi: 10.1104/pp.61.4.581

Auxin Receptors of Maize Coleoptile Membranes Do Not Have ATPase Activity 1

John W Cross 1,2, Winslow R Briggs 1,2, Ulrike C Dohrmann 1,2,2, Peter M Ray 1,2
PMCID: PMC1091921  PMID: 16660340

Abstract

Membrane-localized auxin-binding sites from coleoptiles and primary leaves of Zea mays L. which may be auxin receptors can be fully solubilized by 1 to 1.5 mg of Triton X-100 per mg of membrane protein (about 1 mg per gram of original tissue fresh weight), while 70% of the basal (Mg2+)-ATPase and 85% of the K+-stimulated (Mg2+)-ATPase (pH 6) remain pelletable. Gel exclusion chromatography on Bio-Gel A-1.5m indicates that the solubilized receptors occur as detergent-protein micelles of about 90,000 daltons equivalent molecular weight. Solubilized ATPase activities occur (a) as very large particles excluded from the gel, and (b) as particles of a size substantially smaller than the particles that exhibit auxin binding. The auxin-binding receptor therefore appears not to be an ATPase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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