Biochemical similarities between soluble and membrane-bound calcium-dependent protein kinases of barley

Journal Article · Sun Apr 01 00:00:00 EST 1990 · Plant Physiology; (USA)

DOI:https://doi.org/10.1104/pp.92.4.919· OSTI ID:5925806

Klimczak, L J; Hind, G ^[1]

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1. Brookhaven National Laboratory, Upton, NY (USA)

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 {plus minus} 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.

• OSTI ID: 5925806
• Journal Information: Plant Physiology; (USA), Vol. 92:4; ISSN 0032-0889
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PHOSPHOTRANSFERASES
BIOCHEMICAL REACTION KINETICS
BARLEY
CALCIUM
MEMBRANE PROTEINS
ALKALINE EARTH METALS
CEREALS
ELEMENTS
ENZYMES
GRASS
KINETICS
LILIOPSIDA
MAGNOLIOPHYTA
METALS
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
PLANTS
PROTEINS
REACTION KINETICS
TRANSFERASES
550200* - Biochemistry