Dissociation of polysome aggregates by protease k.

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 MgCl(2) 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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Larkins BA,Tsai CY

doi

10.1104/pp.60.4.482

subject

Has Abstract

pub_date

1977-10-01 00:00:00

pages

482-5

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

60

pub_type

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