What question did this study set out to answer?

Investigate the phosphorylation of ribosomal proteins and characterize endogenous ribosomal protein kinase activity in a rabbit reticulocyte cell-free system.

January 1, 1971Biochemistry

Phosphorylation of ribosomal proteins in rabbit reticulocytes. A cell-free system with ribosomal protein kinase activity

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Investigate the phosphorylation of ribosomal proteins and characterize endogenous ribosomal protein kinase activity in a rabbit reticulocyte cell-free system.
Developed a cell-free enzymatic assay system derived from rabbit reticulocytes to examine protein modification.
Assayed ribosomal protein kinase activity responsible for transferring phosphate groups to ribosomal proteins in vitro.
Demonstrated active phosphorylation of specific ribosomal proteins mediated by endogenous protein kinase activity.
Established the feasibility of an in vitro cell-free system for characterizing translational machinery modifications.

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Implication

In vitro study demonstrates ribosomal protein phosphorylation in rabbit reticulocytes, indicating enzymatic regulation of protein synthesis machinery.

Cite This Study

David Kabat (1971) studied this question.

synapsesocial.com/papers/6a834ad0f94fbaec1e13236e https://doi.org/10.1021/bi00778a001

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Implication

In vitro study demonstrates ribosomal protein phosphorylation in rabbit reticulocytes, indicating enzymatic regulation of protein synthesis machinery.

Phosphorylation of ribosomal proteins in rabbit reticulocytes. A cell-free system with ribosomal protein kinase activity

Key Points

Discussion

Implication

Cite This Study

Phosphorylation of ribosomal proteins in rabbit reticulocytes. A cell-free system with ribosomal protein kinase activity

Key Points

Discussion

Implication

Cite This Study

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