Open AccessTissue-specific expression of mRNAs for dipeptidyl carboxypeptidase isoenzymes.
Author(s) -
Hamza A. El-Dorry,
Cecil B. Pickett,
John S. MacGregor,
Richard L. Soffer
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.14.4295
Subject(s) - reticulocyte , carboxypeptidase , rna , biochemistry , messenger rna , biology , enzyme , microbiology and biotechnology , isozyme , dipeptidyl peptidase , chemistry , gene
The molecular weight of newly synthesized dipeptidyl carboxypeptidase (angiotensin-converting enzyme; peptidyldipeptide hydrolase, EC 3.4.15.1) polypeptide primed in a reticulocyte lysate by poly(A)-containing RNA from mature rabbit testis was only about 65% that of the immunologically related species programmed by pulmonary RNA. Furthermore, in contrast to the pulmonary RNA-dependent product, the synthesis of this testicular protein was not directed by RNA from testes of immature animals. These findings indicate that a shorter polypeptide chain and pubertal expression--the structural and regulatory properties that distinguish the testicular dipeptidyl carboxypeptidase isozyme--are determined pretranslationally.