Western blot analysis of cereal grain prolamins using an antibody to carboxyl-linked indoleacetic acid

• Published in: Plant physiology (Bethesda) Vol. 96; no. 4; pp. 1076 - 1078
• Main Authors: Leverone, L.A, Stroup, T.L, Caruso, J.L
• Format: Journal Article
• Language: English
• Published: Rockville, MD American Society of Plant Physiologists 01.08.1991
• Subjects: Antibodies; Auxins; Avena sativa; Biological and medical sciences; Cellular and Structural Biology; Cereal grains; Corn; Endosperm; Fundamental and applied biological sciences. Psychology; Gels; Growth regulators; indole acetic acid; Indoleacetic acids; Insulin antibodies; Metabolism; Monoclonal antibodies; Pennisetum glaucum; Plant physiology and development; Plants; prolamins; protein composition; seeds; Sorghum bicolor; Zea mays; zein; Avena sativa; Monocotyledones; Storage protein; Auxin; Zea mays; Immunological method; Sorghum bicolor; Gramineae; Angiospermae; Plant growth substance; Spermatophyta; Caryopsis; Conjugated compound; Prolamin
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.96.4.1076

A monoclonal antibody raised against carboxyl-linked IAA was used in Western blot analysis of storage proteins from kernels of Avene sativa, Pennisetum americanum, Sorghum bicolor, and Zea mays. IAA or an IAA-like molecule is associated with the ethanol-soluble protein fraction of the seed. Western blotting of commercial zein, the major storage protein of maize, along with physicochemical evidence reported by Leverone et al. ([1991] Plant Physiol, 96: 1070-1075) indicated that IAA is linked with this prolamin. Results suggest that an IAA-prolamin association may be widespread throughout the Poaceae.