Abstract: The present inventors isolated and purified elicitor-binding proteins in good yield by combining the development of a column that uses APEA derivatives, pre-columns to remove non-specifically adsorbing substances, and effective elution methods. Using the N-terminal and internal chain amino acid sequences of the obtained proteins, the present inventors successfully isolated cDNAs encoding the proteins of the present invention from a rice cDNA library. Moreover, when anti-Con A-CEBiP antibodies were purified and their effect on elicitor-responsive reactive oxygen production was examined, production of reactive oxygen was inhibited by a pretreatment with the antibodies, suggesting that the present proteins are receptor proteins involved in chitin oligosaccharide elicitor responses. Since these elicitors induce resistance to blast in rice, the proteins of the present invention can be applied to the development of novel disease control technologies.

Abstract: A purpose of the present invention is to clarify the mechanism of the intrinsic clotting system which is induced by activation of blood coagulation factor IX by erythrocyte membrane, and to clarify the structure of a factor which activates blood coagulation factor IX by isolating and identifying the factor.

Abstract: Disclosed are peptides represented by IVC1SLC2SC3TAW and C1SLC2SC3 wherein I stands for isoleucine, V for valine, C1 for cysteine, C2 for cysteinesulfinic acid, C3 for cysteinesulfenic acid, S for serine, L for leucine, T for threonine, A for alanine, and W for tryptophan. These peptides can impart photoreactivity to a protein by binding to a non-heme iron. Also disclosed are methods for imparting photoreactivity to cells by introducing the peptide sequences into at least one protein which is involved in a metabolic system and/or energy metabolic system of the cells. There can be provided peptide sequences with a shorter peptide chain capable of imparting photoreactivity, which can be easily introduced into a protein with a little risk in degrading original function of the protein. There are also provided methods enabling control of metabolic reactions by imparting photoreactivity to cells with the peptides.

Abstract: A purpose of the present invention is to clarify the mechanism of the intrinsic clotting system which is induced by activation of blood coagulation factor IX by erythrocyte membrane, and to clarify the structure of a factor which activates blood coagulation factor IX by isolating and identifying the factor.

Abstract: Disclosed are peptides represented by IVC1SLC2SC3TAW and C1SLC2SC3 wherein I stands for isoleucine, V for valine, C1 for cysteine, C2 for cysteinesulfinic acid, C3 for cysteinesulfenic acid, S for serine, L for leucine, T for threonine, A for alanine, and W for tryptophan. These peptides can impart photoreactivity to a protein by binding to a non-heme iron. Also disclosed are methods for imparting photoreactivity to cells by introducing the peptide sequences into at least one protein which is involved in a metabolic system and/or energy metabolic system of the cells. There can be provided peptide sequences with a shorter peptide chain capable of imparting photoreactivity, which can be easily introduced into a protein with a little risk in degrading original function of the protein. There are also provided methods enabling control of metabolic reactions by imparting photoreactivity to cells with the peptides.

Abstract: Disclosed are peptides represented by IVC1SLC2SC3TAW and C1SLC2SC3 wherein I stands for isoleucine, V for valine, C1 for cysteine, C2 for cysteinesulfinic acid, C3 for cysteinesulfenic acid, S for serine, L for leucine, T for threonine, A for alanine, and W for tryptophan. These peptides can impart photoreactivity to a protein by binding to a non-heme iron. Also disclosed are methods for imparting photoreactivity to cells by introducing the peptide sequences into at least one protein which is involved in a metabolic system and/or energy metabolic system of the cells. There can be provided peptide sequences with a shorter peptide chain capable of imparting photoreactivity, which can be easily introduced into a protein with a little risk in degrading original function of the protein. There are also provided methods enabling control of metabolic reactions by imparting photoreactivity to cells with the peptides.