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Nucleic Acids Research, 1975, Vol. 2, No. 10 1903-1910
© 1975

Articles

Isolation and in vitro translation of human placental lactogen messenger RNA from human term placenta

C. Hubert and L. Cedard

Laboratoire de Chimie Hormonale, Maternité 123, Bid de Port-Royal, Paris 75014, France

Received September 1, 1975. A messenger activity for HPL was identified in normal human term placentas. The mRNA was translated in rabbit reticulocyte cell-free system. The HPL synthesized was quantified by a specific immunoprecipitation and further identified by electrophoresis on sodium dodecyl sulfate polyacryla-mide gel. The HPL synthesized in the reticulocyte lysate exhibited a molecular weight between 20,000 and 22,000 daltons similar to the active hormone. The messenger RNA activity for HPL corresponded to a sedimentation coefficient of 11–12 S. Furthermore the messenger activity for HPL was preferentially associated with membrane bound polyribosomes than with free polyribosomes.


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