Location of RNase and RNase inhibitor on free cytoplasmic mRNA-protein particles from human placenta

O. Gileadi; H. Lorberboum; N. de Groot; A. A. Hochberg

doi:10.1007/BF00775355

Location of RNase and RNase inhibitor on free cytoplasmic mRNA-protein particles from human placenta

O. Gileadi^*, H. Lorberboum, N. de Groot, A. A. Hochberg

^*Corresponding author for this work

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › peer-review

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Abstract

Free cytoplasmic mRNPs were isolated from human placenta. An activity of RNase was associated with these particles but was mostly inhibited by a labile protein inhibitor. Both RNase and RNase inhibitor were extractable from mRNPs by 0.5 M KCl. The nature of the association of the RNase-RNase inhibitor complex with mRNPs makes it suitable as a putative system for control of expression and turnover of mRNPs and therefore of protein synthesis.

Original language	English
Pages (from-to)	241-244
Number of pages	4
Journal	Molecular Biology Reports
Volume	9
Issue number	4
DOIs	https://doi.org/10.1007/BF00775355
State	Published - Jan 1984

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abstract = "Free cytoplasmic mRNPs were isolated from human placenta. An activity of RNase was associated with these particles but was mostly inhibited by a labile protein inhibitor. Both RNase and RNase inhibitor were extractable from mRNPs by 0.5 M KCl. The nature of the association of the RNase-RNase inhibitor complex with mRNPs makes it suitable as a putative system for control of expression and turnover of mRNPs and therefore of protein synthesis.",

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AU - de Groot, N.

AU - Hochberg, A. A.

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AB - Free cytoplasmic mRNPs were isolated from human placenta. An activity of RNase was associated with these particles but was mostly inhibited by a labile protein inhibitor. Both RNase and RNase inhibitor were extractable from mRNPs by 0.5 M KCl. The nature of the association of the RNase-RNase inhibitor complex with mRNPs makes it suitable as a putative system for control of expression and turnover of mRNPs and therefore of protein synthesis.

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Location of RNase and RNase inhibitor on free cytoplasmic mRNA-protein particles from human placenta

Abstract

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