z-logo
open-access-imgOpen Access
Synthesis of the Small Subunit of Ribulose-1,5-bisphosphate Carboxylase by Soluble Fraction Polyribosomes of Pea Leaves
Author(s) -
Harry Roy,
Barry Terenna,
Loretta Cheong
Publication year - 1977
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.60.4.532
Subject(s) - polysome , ribulose 1,5 bisphosphate , pisum , biochemistry , isoelectric focusing , rubisco , protein subunit , pyruvate carboxylase , biology , ribulose , isoelectric point , rna , enzyme , ribosome , gene
The products of amino acid incorporation by pea (Pisum sativum L.) leaf soluble fraction polyribosomes in the wheat germ system were examined by two-dimensional electrophoresis and fluorography.There are two isoelectric variants of the small subunit of ribulose bisphosphate carboxylase in this organism, and the more alkaline of these is consistently labeled in the cell-free protein-synthesizing system. The more acid variant is also labeled, but often less extensively. A minority of leaf polyribosomes are recovered from low speed sedimentable fractions. While these appear also to synthesize the small subunits, the patterns of labeling do not indicate a preferential synthesis of these polypeptides by the sedimentable fraction polyribosomes.In the same experiments, labeling of the large subunit spots was sharply below background; these results confirm a cytoplasmic site of synthesis for small subunits of ribulose bisphosphate carboxylase.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom