Eisai Company, Limited

Eisai R&d Management Co., Ltd.

Yoshiya Oda

Yutaka Yoshida

Tadashi Sato

Naoki Asakawa

Tsuyoshi Tabata

Nariyasu Mano

Toshinobu Miwa

Yasushi Ishihama

Hiroyuki Katayama

Hiroshi Ohe

Yukuo Nezu

A method for analyzing a binding ability of protein to a compound, comprising the steps of (a) fractionating a first group of isotope-labeled proteins into plural fractions using a carrier having the compound immobilized thereon; (b) fractionating a second group of proteins into one or plural fractions using a carrier having the compound immobilized thereon; (c) adding an amount of at least one fraction obtained in step (b) to each of the fractions obtained in step (a); (d) analyzing the fractions obtained in step (c) with mass spectrometry; and (e) based on the mass spectrometry information, obtaining, regarding each fraction, an intensity ratio between a peak derived from a protein in the fraction obtained in step (a) and a peak derived from a protein in the fraction obtained in step (b), and comparing degrees of the binding ability of the plural kinds of proteins to the compound.

Method for analysis of compound-binding ability of protein

A method for detecting plural types of phosphorylated proteins in a sample, wherein a database consisting of data regarding plural types of proteins in the sample is used; and a method for purifying phosphorylated proteins using an immobilized metal carrier or a titania carrier, wherein a solution containing acetonitrile in a range of 40% (v/v) or greater but 60% (v/v) or less is used.

Method of proteome analysis for phosphorylated protein

A method for analyzing a structural affinity relationship between plural kinds of proteins and a compound, comprising the steps of (a) using a compound-immobilized carrier to purify plural kinds of proteins bound to the compound on the carrier, from a group of isotope-labeled proteins; (b) using a compound-immobilized carrier to purify plural kinds of proteins bound to the compound on the carrier, from a group of proteins brought into contact with a compound beforehand; (c) mixing the proteins obtained in step (a) and step (b); (d) analyzing the mixture obtained in step (c) with mass spectrometry; (e) identifying each of plural kinds of proteins based on information obtained by the mass spectrometry; and (f) obtaining an intensity ratio between a labeled peak and a non-labeled peak of each protein, thereby quantitating an affinity ratio of the compound to each protein.

Method of analyzing protein structural affinity relationship

An object of the present invention is to quantitate with good accuracy, furthermore, quantitate absolutely, one or a plurality of biological molecules in a sample such as a tissue, a biological fluid, a cell, a cell organ or protein complex. By adding a metabolically isotope labeled biological molecule as an internal standard substance and measuring with a mass spectrometer, quantitating with good accuracy one or a plurality of target molecules in a sample has become possible. In addition, by performing waveform separation processing during mass analysis, a highly accurate quantitative analysis method of mass analysis is provided.

Mass spectrometric quantitation method for biomolecules based on metabolically labeled internal standards

Separating agent comprising bonded conalbumin

A packing for chromatography whereby a low molecular weight substance contained in biological samples can be analyzed directly at a high accuracy without any pretreatments. This packing is combining a protein such as avidin and ovomucoid to the support via a straight or branched spacer optionally having a functional group such as a cyano group. Enantiomers interact differentially with proteins, and thereby optically separated. Further, a purification column packed with said packing is disclosed. According to the present invention, a low molecular weight substance can be directly and accurately analyzed without requiring any pretreatment for removing biological macromolecules. When it is employed in the purification column, the time required for the pretreatment can be shortened.

Packings combining protein to a support via a spacer

The components present in the sample with a mobile phase A in 1st section is separated. In 2nd section there is provided with an inserting line of a dilute solution for diluting the mobile phase A and a trapping column which forces the dilute solution to pass but catches the components by connecting said line to said column. In 3rd section, the components caught by the trapping column are introduced into mass spectrometer by using a mobile phase B. It is preferable to use respectively different mobile phases for the mobile phase A and the mobile phase B. It is good to install separating columns in 1st and 3rd sections. It is also desired to add the retaining apparatus of the components separated in 1st section.

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Tsukuba, Japan

Yoshiya Oda