TOP > 外国特許検索 > ENZYME HAVING ACTIVITY FOR RELEASING GLYCOPROTEIN SUGAR CHAINS AND METHOD FOR PRODUCING SAME, AND METHOD FOR RELEASING SUGAR CHAINS USING SAID ENZYME

ENZYME HAVING ACTIVITY FOR RELEASING GLYCOPROTEIN SUGAR CHAINS AND METHOD FOR PRODUCING SAME, AND METHOD FOR RELEASING SUGAR CHAINS USING SAID ENZYME コモンズ

外国特許コード F140008045
整理番号 S2013-0214-C0
掲載日 2014年12月4日
出願国 世界知的所有権機関(WIPO)
国際出願番号 2013JP081422
国際公開番号 WO 2014080991
国際出願日 平成25年11月21日(2013.11.21)
国際公開日 平成26年5月30日(2014.5.30)
優先権データ
  • 特願2012-255631 (2012.11.21) JP
  • 特願2013-108153 (2013.5.22) JP
発明の名称 (英語) ENZYME HAVING ACTIVITY FOR RELEASING GLYCOPROTEIN SUGAR CHAINS AND METHOD FOR PRODUCING SAME, AND METHOD FOR RELEASING SUGAR CHAINS USING SAID ENZYME コモンズ
発明の概要(英語) The problem is to provide an enzyme that acts on complex sugar chains and has activity for directly releasing sugar chains from glycoproteins themselves. The problem is solved by an enzyme derived from microorganisms selected from the genus Lactobacillus and the genus Prevotella, or having an amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 9, or SEQ ID NO: 11 or an amino acid sequence having at least 70% homology with at least one of these sequences, and having activity for releasing glycoprotein sugar chains.
従来技術、競合技術の概要(英語) BACKGROUND ART
Sugar chain, protein, deoxyribonucleic acid (DNA) 3 followed by the second biometric information molecule referred to as biopolymers. In humans, such as about 10 glucose sugar chain is composed of the monosaccharide type dendritic molecules, most of the proteins bound to glycoproteins and glycolipids present as lipid. Sugar chain, or present in a body fluid as a secreted protein, or membrane protein or glycolipid as often covers the surface of the cells.
A recent study, a wider variety of functions of the sugar chains are revealed. Specifically, sugar chain, cancer (metastasis, such as a tumor marker), immune (immune receptor modulators, immune cell differentiation, such as antibody pharmaceuticals), fertilization, generation, differentiation (such as regenerative medicine), infection (influenza, H. pylori, such as cholera toxin) such as in, play an important role in the currently known. The current, the structure and function of sugar chain by analysis, the diagnosis of cancer or immune disease, development of methods for prophylaxis or treatment, such as the construction of drug delivery system, various fields are expected to be applied to.
Glycoproteins of the sugar chain structure and functional analysis of order, it is necessary to release the sugar chain. Patent Document 1 is, of an aldehyde group on a sugar chain that specifically binds to substances with hydrazide groups, free sugar chains from glycoprotein disclosed is a method. However, in this method, due to the decomposition of the protein moiety. In addition, free of the sugar chain structure is partially changed.
And the protein portion of the carbohydrate moieties without change both the free sugar chains from glycoprotein as a method, also known the method of using a. Specifically, asparagine-type sugar chain releasing enzyme, used worldwide end - β-N - acetylglucosaminidase (hereinafter, simply also referred to as' end ') as, Streptomyces, and derived from end H (Streptomyces plicatus) . However, the end H, yeast and filamentous fungi of the characteristic of a glycoprotein sugar chain asparagine -type and hybrid type N-linked carbohydrate chain acting, higher animals such as a human glycoprotein which is characteristic of a complex-type sugar chain does not act on.
Recent has become commercially available, is derived from end M (Mucor hiemalis), in the same manner as end H, and hybrid-type sugar chain to well in the mold. End M is, complex-type sugar chain acting on the chain 2 by its nature, glycosides are used in the synthesis. However, their action is, lower than -type effect. In addition, carbohydrate moieties and between the stopper and the fucose glycoprotein comprising 3-5 of the sugar chain and complex-type sugar chain is present chain branching does not easily act. Further, in order to free sugar chains, digested with a protein moiety, a sugar or sugar asparagine is necessary. Therefore, the end M may be used, directly free sugar chains from glycoprotein itself is difficult.
  • 出願人(英語)
  • ※2012年7月以前掲載分については米国以外のすべての指定国
  • PUBLIC UNIVERSITY CORPORATION OSAKA CITY UNIVERSITY
  • 発明者(英語)
  • ITO, Kazuo
国際特許分類(IPC)
指定国 National States: AE AG AL AM AO AT AU AZ BA BB BG BH BN BR BW BY BZ CA CH CL CN CO CR CU CZ DE DK DM DO DZ EC EE EG ES FI GB GD GE GH GM GT HN HR HU ID IL IN IR IS JP KE KG KN KP KR KZ LA LC LK LR LS LT LU LY MA MD ME MG MK MN MW MX MY MZ NA NG NI NO NZ OM PA PE PG PH PL PT QA RO RS RU RW SA SC SD SE SG SK SL SM ST SV SY TH TJ TM TN TR TT TZ UA UG US UZ VC VN ZA ZM ZW
ARIPO: BW GH GM KE LR LS MW MZ NA RW SD SL SZ TZ UG ZM ZW
EAPO: AM AZ BY KG KZ RU TJ TM
EPO: AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LT LU LV MC MK MT NL NO PL PT RO RS SE SI SK SM TR
OAPI: BF BJ CF CG CI CM GA GN GQ GW KM ML MR NE SN TD TG

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