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. 1977 Oct;60(4):482–485. doi: 10.1104/pp.60.4.482

Dissociation of Polysome Aggregates by Protease K 1

Brian A Larkins a, C Y Tsai a
PMCID: PMC542646  PMID: 16660120

Abstract

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.

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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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