Purification of a bovine liver S6 kinase Journal Article


Authors: Tabarini, D.; Garcia de Herreros, A.; Heinrich, J.; Rosen, O. M.
Article Title: Purification of a bovine liver S6 kinase
Abstract: A bovine liver protein serine kinase that catalyzes the multisite phosphorylation of ribosomal protein S6 has been purified to near homogeneity. The enzyme has an Mr of 67,000 on SDS-polyacrylamide gel electrophoresis and an apparent molecular weight of 55,000 on glycerol gradient sedimentation. Its enzymic properties, substrate specificity, molecular size and chromatographic behaviour are similar to those of the principal growth factor - and phorbol 12-myristate 13-acetate-stimulated S6 kinase of cultures cells. © 1987 Academic Press, Inc.
Keywords: nonhuman; methodology; animal cell; animal; protein kinases; liver; kinetics; substrate specificity; cattle; molecular weight; protein kinase; enzyme purification; ribosomal proteins; ribosome protein; ribosomal protein s6 kinases; protein serine kinase; priority journal; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
Journal Title: Biochemical and Biophysical Research Communications
Volume: 144
Issue: 2
ISSN: 0006-291X
Publisher: Elsevier Science, Inc.  
Date Published: 1987-04-29
Start Page: 891
End Page: 899
Language: English
DOI: 10.1016/s0006-291x(87)80048-7
PUBMED: 3579946
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 5 February 2021 -- Source: Scopus; Acknowledgments: The authors wish to thank Karen Carr for her excellent technical assistance in the preparation of 40S ribosomal subunits.
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  1. Ora Mendelsohn Rosen
    58 Rosen