Subunit Structure and Composition of Oat Seed Globulin
- 1 October 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 62 (4) , 506-509
- https://doi.org/10.1104/pp.62.4.506
Abstract
Oat (Avena sativa L.) seed globulin was extracted from ground caryopses with 1 M NaCl, 0.05 M Tris(hydroxymethyl)aminoethane (ph 8.5) at room temperature. The globulin had a sedimentation constant of 12.1, and a MW of 322,000, as determined by analytical ultracentrifugation. The globulin could be separated into 2 major subunits by sodium-dodecyl sulfate polyacrylamide gel electrophoresis. MW of the subunits were 21,700 (.alpha.) and 31,700 (.beta.), and they were present in equimolar amounts. A subunit model of 6.alpha. and 6.beta. per molecule of globulin is proposed. Amino acid analysis indicated that the .alpha. subunit contained more basic amino acids and aspartic acid/asparagine but less glutamic acid/glutamine and glycine than the .beta. subunit.This publication has 14 references indexed in Scilit:
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