shown within the concentration change of calcium ion in artificial membrane system.
Protein kinase C has hydrophobic region in its structure, but it exists in cytoplasm in
resting state, and binds to plasma membrane in calcium concentration dependent
manner by stimulation through receptor. Protein kinase C was partially purified from
neutrophil of leucocyte and cell membranes of the neutrophil were incubated at
various concentrations of calcium ion, and then the membrane fraction and supernatant was separated by centrifugation. And distribution of the protein kinase C was
investigated after removal of calcium ions by EDTA and activation by Triton X-100.
The result showed that the protein kinase C bound to the cell membranes at a few μM
of calcium ion [20]. Relationship between surface pressure of monolayer and
binding of protein kinase C to the monolayer was investigated at the presence of
calcium ion at various surface pressures. The protein kinase C penetrated the
monolayer only in the presence of calcium ion when the surface pressure was
more than 26 dyn/cm, but the protein kinase C bound to the monolayer below
26 dyn/cm in the absence of calcium ion. However, the protein kinase C did not
bind to the monolayer at concentration of calcium ion more than 43 dyn/cm even in
the presence of calcium ion [21]. From the results shown above, electrostatic and
hydrophobic interactions for role of protein kinase C in the signaling system are
supposed as follows. Base sequence of cDNA including 672 amino acid sequences
was elucidated in protein kinase C [22]. Protein kinas C has amino acids sequence of
Arg19-Phe-Ala-Arg-Lys-Gly-Ala25-Leu-Arg-Gln-Lys-Asn-Val-His-Glu-Val-Lys-Asn
Fig. 6.3 Metabolic conversion of membrane lipids
Phosphatidylinositol cycle in a cell is shown. Diacylglycerol (DG) and inositol triphosphate (ITP)
are generated from phosphatidylinositol bisphosphate (PIP2) in phosphatidylinositol cycle in
metabolic conversion of biomembrane lipids. DG activates protein kinase C and ITP releases
calcium ions from microsomes
86
6 Physical Properties of Biomembranes and Cellular Functions
Protein kinase C has hydrophobic region in its structure, but it exists in cytoplasm in
resting state, and binds to plasma membrane in calcium concentration dependent
manner by stimulation through receptor. Protein kinase C was partially purified from
neutrophil of leucocyte and cell membranes of the neutrophil were incubated at
various concentrations of calcium ion, and then the membrane fraction and supernatant was separated by centrifugation. And distribution of the protein kinase C was
investigated after removal of calcium ions by EDTA and activation by Triton X-100.
The result showed that the protein kinase C bound to the cell membranes at a few μM
of calcium ion [20]. Relationship between surface pressure of monolayer and
binding of protein kinase C to the monolayer was investigated at the presence of
calcium ion at various surface pressures. The protein kinase C penetrated the
monolayer only in the presence of calcium ion when the surface pressure was
more than 26 dyn/cm, but the protein kinase C bound to the monolayer below
26 dyn/cm in the absence of calcium ion. However, the protein kinase C did not
bind to the monolayer at concentration of calcium ion more than 43 dyn/cm even in
the presence of calcium ion [21]. From the results shown above, electrostatic and
hydrophobic interactions for role of protein kinase C in the signaling system are
supposed as follows. Base sequence of cDNA including 672 amino acid sequences
was elucidated in protein kinase C [22]. Protein kinas C has amino acids sequence of
Arg19-Phe-Ala-Arg-Lys-Gly-Ala25-Leu-Arg-Gln-Lys-Asn-Val-His-Glu-Val-Lys-Asn
Fig. 6.3 Metabolic conversion of membrane lipids
Phosphatidylinositol cycle in a cell is shown. Diacylglycerol (DG) and inositol triphosphate (ITP)
are generated from phosphatidylinositol bisphosphate (PIP2) in phosphatidylinositol cycle in
metabolic conversion of biomembrane lipids. DG activates protein kinase C and ITP releases
calcium ions from microsomes
86
6 Physical Properties of Biomembranes and Cellular Functions