This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Web of Science (9) Citing Articles via Google Scholar Google Scholar Articles by Larkins, B. A. Articles by Tsai, C. Y. Search for Related Content PubMed PubMed Citation Articles by Larkins, B. A. Articles by Tsai, C. Y. Agricola Articles by Larkins, B. A. Articles by Tsai, C. Y.

Articles

Dissociation of Polysome Aggregates by Protease K ¹

^a Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907

Apparent large size-classes of zein-synthesizing polysomes from developing kernels of Zea mays L. were converted to smaller polysomes after treatment with Protease K. The reduction in polysome size was not a result of ribonuclease activity, inasmuch as the enzyme did not affect the free polysomes or the size of the mRNA from the membrane-bound polysomes. High concentrations of MgCl₂ in polysome buffer inhibited ribonuclease activity and appeared to cause protein interaction between nascent zein polypeptides. Although Protease K inhibited the polysome's capacity for protein synthesis, it was a useful reagent for determining if polysomes were aggregated by protein.