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

@article{citeulike:5425773, abstract = {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. 10.1104/pp.92.4.919}, author = {Klimczak, Leszek J. and Hind, Geoffrey}, citeulike-article-id = {5425773}, citeulike-linkout-0 = {http://dx.doi.org/10.1104/pp.92.4.919}, citeulike-linkout-1 = {http://www.plantphysiol.org/cgi/content/abstract/92/4/919}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16667406}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16667406}, day = {1}, doi = {10.1104/pp.92.4.919}, journal = {Plant Physiol.}, keywords = {soluble}, month = {April}, number = {4}, pages = {919--923}, posted-at = {2009-08-12 09:03:31}, priority = {2}, title = {Biochemical Similarities between Soluble and Membrane-Bound Calcium-Dependent Protein Kinases of Barley}, url = {http://dx.doi.org/10.1104/pp.92.4.919}, volume = {92}, year = {1990} }

TY - JOUR ID - citeulike:5425773 L3 - citeulike-article-id:5425773 N2 - 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. 10.1104/pp.92.4.919 IS - 4 JF - Plant Physiol. EP - 923 TI - Biochemical Similarities between Soluble and Membrane-Bound Calcium-Dependent Protein Kinases of Barley VL - 92 SP - 919 KW - soluble AU - Klimczak, Leszek AU - Hind, Geoffrey PY - 1990/04/01/ UR - http://dx.doi.org/10.1104/pp.92.4.919 ER -