Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 92:919-923 (1990)
© 1990 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (32)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Klimczak, L. J.
Right arrow Articles by Hind, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klimczak, L. J.
Right arrow Articles by Hind, G.
Agricola
Right arrow Articles by Klimczak, L. J.
Right arrow Articles by Hind, G.
Metabolism and Enzymology

Biochemical Similarities between Soluble and Membrane-Bound Calcium-Dependent Protein Kinases of Barley 1

Leszek J. Klimczak and Geoffrey Hind

Biology Department, Upton, New York 11973, Brookhaven National Laboratory, Upton, New York 11973

The soluble and membrane-bound forms of the calcium-dependent protein kinase from barley leaves (Hordeum vulgare L. cv. Borsoy) have been partially purified and compared. Both forms showed an active polypeptide of 37 kilodaltons on activity gels with incorporated histone as substrate. They eluted from chromatofocusing columns at an identical isoelectric point of pH 4.25 ± 0.2, and also comigrated on several other chromatographic affinity media including Matrex Gel Blue A, histone-agarose, phenyl-Sepharose, and heparin-agarose. Both activities comigrated with chicken ovalbumin during gel filtration through Sephacryl S-200, indicating a native molecular mass of 45 kilodaltons. The activities share a number of enzymatic properties including salt and pH dependence, free calcium stimulation profile, substrate specificity, and Km values. The soluble activity was shown to bind to artificial lipid vesicles. These data suggest strongly that the soluble and membrane-bound calcium-dependent protein kinases from barley are very closely related or even identical.

1 This research was carried out at Brookhaven National Laboratory under the auspices of the U.S. Department of Energy and with funding from its Office of Basic Energy Sciences, Division of Energy Biosciences.




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
S. X. Lu and E. M. Hrabak
An Arabidopsis Calcium-Dependent Protein Kinase Is Associated with the Endoplasmic Reticulum
Plant Physiology, March 1, 2002; 128(3): 1008 - 1021.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1990 by the American Society of Plant Biologists