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A Secondary Processing Site in the Precursor of the Small Subunit of Ribulose Bisphosphate Carboxylase of Chlamydomonas reinhardtii y-1
Author(s) -
Dawn B. Marks,
Barbara Keller,
J. Kenneth Hoober
Publication year - 1986
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.81.2.702
Subject(s) - chlamydomonas reinhardtii , ribulose 1,5 bisphosphate , pyruvate carboxylase , rubisco , chlamydomonas , protein subunit , biochemistry , biology , chemistry , microbiology and biotechnology , enzyme , gene , mutant
When the precursor of ribulose bisphosphate carboxylase of Chlamydomonas reinhardtii y-1 is bound to antibodies and treated with the soluble cell fraction, it is cleaved to the mature form (M(r) 16,500) via an intermediate of M(r) 18,500. Although this intermediate has only been observed in vitro, it may be produced during processing of the precursor in vivo.

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