Tissue-specific expression of mRNAs for dipeptidyl carboxypeptidase isoenzymes.
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.
D000818:Animals; D002474:Cell-Free System; D005786:Gene Expression Regulation; D007527:Isoenzymes / Q000235:genetics*; D008168:Lung / Q000201:enzymology; D008297:Male; D008970:Molecular Weight; D009928:Organ Specificity; D007703:Peptidyl-Dipeptidase A / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics*; D011817:Rabbits; D012741:Sexual Maturation; D013737:Testis / Q000201:enzymology
D007527:Isoenzymes; D012333:RNA, Messenger; D007703:Peptidyl-Dipeptidase A