Auxin receptors of maize coleoptile membranes do not have ATPase activity.

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 (Mg(2+))-ATPase and 85% of the K(+)-stimulated (Mg(2+))-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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Cross JW,Briggs WR

doi

10.1104/pp.61.4.581

subject

Has Abstract

pub_date

1978-04-01 00:00:00

pages

581-4

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

61

pub_type

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