Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations

Purified S6/H4 kinase (Mr 60,000) requires autophosphorylation for activation. A rabbit anti-S6/H4 kinase peptide (SVIDPVPAPVGDSHVDGAAK) antibody recognized both the S6/H4 kinase holoenzyme and catalytic domain. Immunoreactivity with p60 kinase protein, and S6/H4 kinase activity were precisely corre...

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Main Author: Taylor, Allison Antoinette
Other Authors: Masaracchia, Ruthann A.
Format: Others
Language:English
Published: University of North Texas 1998
Subjects:
Online Access:https://digital.library.unt.edu/ark:/67531/metadc501281/
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spelling ndltd-unt.edu-info-ark-67531-metadc5012812017-03-17T08:41:16Z Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations Taylor, Allison Antoinette protein kinases phosphorylation lymphomas Protein kinases. Phosphorylation. Lymphomas. Purified S6/H4 kinase (Mr 60,000) requires autophosphorylation for activation. A rabbit anti-S6/H4 kinase peptide (SVIDPVPAPVGDSHVDGAAK) antibody recognized both the S6/H4 kinase holoenzyme and catalytic domain. Immunoreactivity with p60 kinase protein, and S6/H4 kinase activity were precisely correlated in fractions obtained from ion exchange chromatography of P1798 lymphosarcoma extracts. An enzyme which catalyzed the MgATP-dependent phosphorylation and activation of S6/H4 kinase coeluted with immunoreactivity from Mono 5, but not Mono Q chromatography. Since S6/H4 kinase is homologous with rac-activated PAK65, the observation that phosphorylation is also required for activation suggests a complex mechanism for in vivo activation of the S6/H4 kinase. University of North Texas Masaracchia, Ruthann A. Benjamin, Robert C. Norton, S. J. 1998-12 Thesis or Dissertation x, 67 leaves : ill. Text call-no: 379 N81 no.7575 untcat: b2136793 local-cont-no: 1002660031-Taylor_COLOR https://digital.library.unt.edu/ark:/67531/metadc501281/ ark: ark:/67531/metadc501281 English Public Copyright Copyright is held by the author, unless otherwise noted. All rights reserved. Taylor, Allison Antoinette
collection NDLTD
language English
format Others
sources NDLTD
topic protein kinases
phosphorylation
lymphomas
Protein kinases.
Phosphorylation.
Lymphomas.
spellingShingle protein kinases
phosphorylation
lymphomas
Protein kinases.
Phosphorylation.
Lymphomas.
Taylor, Allison Antoinette
Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
description Purified S6/H4 kinase (Mr 60,000) requires autophosphorylation for activation. A rabbit anti-S6/H4 kinase peptide (SVIDPVPAPVGDSHVDGAAK) antibody recognized both the S6/H4 kinase holoenzyme and catalytic domain. Immunoreactivity with p60 kinase protein, and S6/H4 kinase activity were precisely correlated in fractions obtained from ion exchange chromatography of P1798 lymphosarcoma extracts. An enzyme which catalyzed the MgATP-dependent phosphorylation and activation of S6/H4 kinase coeluted with immunoreactivity from Mono 5, but not Mono Q chromatography. Since S6/H4 kinase is homologous with rac-activated PAK65, the observation that phosphorylation is also required for activation suggests a complex mechanism for in vivo activation of the S6/H4 kinase.
author2 Masaracchia, Ruthann A.
author_facet Masaracchia, Ruthann A.
Taylor, Allison Antoinette
author Taylor, Allison Antoinette
author_sort Taylor, Allison Antoinette
title Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
title_short Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
title_full Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
title_fullStr Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
title_full_unstemmed Regulation of an S6/H4 Kinase in Crude Lymphosarcoma P1798 Preparations
title_sort regulation of an s6/h4 kinase in crude lymphosarcoma p1798 preparations
publisher University of North Texas
publishDate 1998
url https://digital.library.unt.edu/ark:/67531/metadc501281/
work_keys_str_mv AT taylorallisonantoinette regulationofans6h4kinaseincrudelymphosarcomap1798preparations
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