| 序号 | 专利名 | 申请号 | 申请日 | 公开（公告）号 | 公开（公告）日 | 发明人 |
|---|---|---|---|---|---|---|
| 1 | 肽基甘氨肽α酰胺化单氧加氧酶(PAM)用于C端酰胺化的用途 | CN201480066822.8 | 2014-12-10 | CN105793278A | 2016-07-20 | E·霍夫曼; G·蒂芬塔勒 |
| 本文公开的一个方面是，用于对多肽进行体内C端酰胺化的方法，其特征在于，(待酰胺化)多肽和人肽基甘氨肽α?酰胺化单氧加氧酶(PAM)在哺乳动物细胞中重组共表达。 | ||||||
| 2 | 在用于蛋白质表达的细胞系中减少酰胺化的氨基酸形成 | CN201380020180.3 | 2013-04-16 | CN104903447A | 2015-09-09 | 米哈埃拉·斯库利; 多米尼克·戈赛尔 |
| 本发明涉及一种在给定的细胞系中降低肽酰胺化的方法，具有肽酰胺化活性降低的细胞系及其相关应用。 | ||||||
| 3 | USE OF PEPTIDYLGLYCINE ALPHA-AMIDATING MONOOXIGENASE (PAM) FOR C-TERMINAL AMIDATION | US15185477 | 2016-06-17 | US20160333386A1 | 2016-11-17 | EIKE HOFFMANN; GEORG TIEFENTHALER |
| One aspect as reported herein is a method for in vivo C-terminal amidation of a polypeptide characterized in that both the polypeptide (to be amidated) and human peptidylglycine alpha-amidating monooxigenase (PAM) are recombinantly co-expressed in a mammalian cell. | ||||||
| 4 | Enzymatic reactions in the presence of keto acids | US11285136 | 2005-11-22 | US07445911B2 | 2008-11-04 | Angelo P. Consalvo; Nozer M. Mehta; William Stern; James P. Gilligan |
| Conversion in vitro of X-Gly to X-alpha-hydroxy-Gly or X—NH2 (X being a peptide or any other compound having a carbonyl group capable of forming a covalent bond with glycine) is accomplished enzymatically in the presence of keto acids, or salts or esters thereof, to provide a good yield without the necessity of catalase or similar enzymatic reaction enhancers. Peptidylglycine α-amidating monooxygenase (PAM) is a preferred enzyme for catalyzing the conversion. Alternatively, peptidylglycine α-hydroxylating monooxygenase (PHM) is utilized to convert X-Gly to X-alpha-hydroxy-Gly which may be recovered, or optionally may be simultaneously or sequentially converted to an amide by either a Lewis base or action of the enzyme peptidyl α-hydroxyglycine α-amidating lyase (PAL). Both PHM and PAL are functional domains of PAM. | ||||||
| 5 | Alpha-amidating enzyme compositions and processes for their production and use | US07086161 | 1987-08-14 | US06319685B1 | 2001-11-20 | James P. Gilligan; Barry N. Jones |
| Purified enzymatic compositions are provided having alpha-amidating enzymes capable of catalyzing the conversion of a peptidyl compound having a C-terminal glycine residue to a corresponding peptidyl amide having an amino group in place of the C-terminal glycine. The purified compositions have specific activities above 25 mU per mg protein and are sufficiently free of proteases to allow effective catalysis of even peptidyl compounds having L-amino acids. Biologically important alpha-amidated products such as calcitonin and other regulatory hormones are efficiently produced using the alpha-amidation reaction catalyzed by the enzymes. Purification by size exclusion chromatography in combination with strong anion exchange chromatography results in homogeneous enzyme species which are used to prepare antibodies specific for the alpha-amidating enzyme. A gene capable of expressing the alpha-amidating enzyme is ligated into an expression vector and transformed into a host cell capable of expressing the gene. | ||||||
| 6 | Recombinant C-terminal .alpha.-amidating enzyme | US759184 | 1996-12-04 | US5821083A | 1998-10-13 | Kazuhiro Ohsuye; Katsuhiko Kitano; Shoji Tanaka; Hisayuki Matsuo; Kensaku Mizuno |
| A C-terminal .alpha.-amidating enzyme of Xenopus laevis and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal .alpha.-amidated peptide using the enzyme. | ||||||
| 7 | C-terminal .alpha.-amidating enzyme and process for production thereof | US921600 | 1992-08-03 | US5360727A | 1994-11-01 | Hisayuki Matsuo; Kensaku Mizuno; Masayasu Kojima |
| The invention relates to a C-terminal .alpha.-amidating enzyme of porcine origin having the following properties: (1) the action is on a peptide or protein represented by the formula:X-R-Gly,wherein Gly represents a C-terminal glycine residue, R represents an amino acid residue to be .alpha.-amidated, and X represents a remaining portion of the peptide or protein to convert it to a peptide or protein represented by the formula:X-R-NH.sub.2,wherein R-NH.sub.2 represents a C-terminal .alpha.-amidated amino acid residue and X represents a remaining portion of the peptide or protein; (2) the optimal pH is 6.5 to 8.5; (3) the molecular weight is about 92,000 as determined by SDS-polyacrylamide gel electrophoresis; and (4) it contains the following peptide fragment:. . . Glu-Ala-Pro-Leu-Leu-Ile-Leu-Gly . . . .Further, the invention relates to a process for the production of the C-terminal .alpha.-amidating enzyme comprising the steps of extracting and purifying the enzyme from porcine atrium cordis exhibiting the enzyme activity. | ||||||
| 8 | .alpha.-amidation enzyme | US655366 | 1984-09-27 | US4708934A | 1987-11-24 | James P. Gilligan; Barry N. Jones |
| Peptidyl-glycine .alpha.-amidating monooxygenase is an enzyme extractable from medullary thyroid carcinoma cell lines and tissue samples, having a molecular mass of about 60,000 to 65,000 daltons. It has been purified so as to exhibit a single, homogeneous, well-defined band using electrophoretic procedures performed on SDS-polyacrylamide gels, and has a specific enzymatic activity of at least 50 mU per mg protein. The free or immobilized enzyme, in the presence of Cu.sup.+2 ions, ascorbate, and oxygen, can be used to prepare an .alpha.-amidated protein from a polypeptide substrate possessing a carboxyl-terminal glycine residue. The purified enzyme can be used as an antigen in order to produce enzyme-specific monoclonal antibodies, and can provide the information necessary to design and construct prokaryotes or other appropriate unicellular organisms or host cells isolated from multicellular organisms which possess peptidyl-glycine .alpha.-amidating capability. | ||||||
| 9 | Enzymatic reactions in the presence of keto acids | US12284552 | 2008-09-22 | US08163871B2 | 2012-04-24 | Angelo P. Consalvo; Nozer M. Mehta; William Stern; James P. Gilligan |
| Conversion in vitro of X-Gly to X-alpha-hydroxy-Gly or X-NH2 (X being a peptide or any other compound having a carbonyl group capable of forming a covalent bond with glycine) is accomplished enzymatically in the presence of keto acids, or salts or esters thereof, to provide a good yield without the necessity of catalase or similar enzymatic reaction enhancers. Peptidylglycine α-amidating monooxygenase (PAM) is a preferred enzyme for catalyzing the conversion. Alternatively, peptidylglycine α-hydroxylating monooxygenase (PHM) is utilized to convert X-Gly to X-alpha-hydroxy-Gly which may be recovered, or optionally may be simultaneously or sequentially converted to an amide by either a Lewis base or action of the enzyme peptidyl α-hydroxyglycine α-amidating lyase (PAL). Both PHM and PAL are functional domains of PAM. | ||||||
| 10 | Enzymatic reactions in the presence of keto acids | US12284552 | 2008-09-22 | US20090023892A1 | 2009-01-22 | Angelo P. Consalvo; Nozer M. Mehta; William Stern; James P. Gilligan |
| Conversion in vitro of X-Gly to X-alpha-hydroxy-Gly or X-NH2 (X being a peptide or any other compound having a carbonyl group capable of forming a covalent bond with glycine) is accomplished enzymatically in the presence of keto acids, or salts or esters thereof, to provide a good yield without the necessity of catalase or similar enzymatic reaction enhancers. Peptidylglycine α-amidating monooxygenase (PAM) is a preferred enzyme for catalyzing the conversion. Alternatively, peptidylglycine α-hydroxylating monooxygenase (PHM) is utilized to convert X-Gly to X-alpha-hydroxy-Gly which may be recovered, or optionally may be simultaneously or sequentially converted to an amide by either a Lewis base or action of the enzyme peptidyl α-hydroxyglycine α-amidating lyase (PAL). Both PHM and PAL are functional domains of PAM. | ||||||
| 11 | Enzymatic reactions in the presence of keto acids | US11285136 | 2005-11-22 | US20060127995A1 | 2006-06-15 | Angelo Consalvo; Nozer Mehta; William Stern; James Gilligan |
| Conversion in vitro of X-Gly to X-alpha-hydroxy-Gly or X—NH2 (X being a peptide or any other compound having a carbonyl group capable of forming a covalent bond with glycine) is accomplished enzymatically in the presence of keto acids, or salts or esters thereof, to provide a good yield without the necessity of catalase or similar enzymatic reaction enhancers. Peptidylglycine α-amidating monooxygenase (PAM) is a preferred enzyme for catalyzing the conversion. Alternatively, peptidylglycine α-hydroxylating monooxygenase (PHM) is utilized to convert X-Gly to X-alpha-hydroxy-Gly which may be recovered, or optionally may be simultaneously or sequentially converted to an amide by either a Lewis base or action of the enzyme peptidyl α-hydroxyglycine α-amidating lyase (PAL). Both PHM and PAL are functional domains of PAM. | ||||||
| 12 | Enzymatic production of a C-terminal &agr;-amidated peptide or protein | US08845381 | 1997-04-25 | US06602681B1 | 2003-08-05 | Kazuhiro Ohsuye; Katsuhiko Kitano; Shoji Tanaka; Hisayuki Matsuo; Kensaku Mizuno |
| A C-terminal &agr;-amidating enzyme of Xenopus laevis and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal &agr;-amidated peptide using the enzyme. | ||||||
| 13 | Recombinant C-terminal &agr;-amidating enzyme | US07219375 | 1988-07-15 | US06262232B1 | 2001-07-17 | Kazuhiro Ohsuye; Katsuhiko Kitano; Shoji Tanaka; Hisayuki Matsuo; Kensaku Mizuno |
| A C-terminal &agr;-amidating enzyme of Xenopus laevis and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal &agr;-amidated peptide using the enzyme. | ||||||
| 14 | cDNA encoding peptidyl-glycine alpha-amidating monooxygenase (PAM) | US07096447 | 1987-09-15 | US06255067B1 | 2001-07-03 | Henry T. Keutmann; Peter Schofield; Henry Rodriguez; Betty Eipper; Richard Mains |
| The sequence of bovine PAM is taught as well as new forms of PAM not known before. One new form is membrane bound and provides the basis of methods for alpha-amidating inactive precursors of peptide hormones. | ||||||
| 15 | C-terminal amidating enzyme composition, process for preparing, and use of the same | US459829 | 1990-01-29 | US5354675A | 1994-10-11 | Toshii Iida; Yuka Fuse; Masahiro Tajima; Mitsuo Yanagi; Hiroshi Okamoto |
| A C-terminal amidating enzyme composition is disclosed having the ability to amidate the C-terminus of peptides with a C-terminal glycine. The C-terminal amidating enzyme is characterized by having a stable pH range of 5 to 9, metal ions and L-ascorbic acid as cofactors, two active fractions at molecular weights of about 50,000 and about 100,000 as determined from gel filtration, isoelectric points of about 4.5 pH for the active fraction having a molecular weight of about 50,000 and about 6.7 pH for the active fraction having a molecular weight of about 100,000 according to isoelectric point chromatography, and is activated by addition of catalase. | ||||||
| 16 | Enzyme and DNA coding therefor | US707367 | 1991-05-30 | US5196316A | 1993-03-23 | Yasuno Iwasaki; Yoshiki Nishikawa |
| The invention concerns a peptidylhydroxyglycine N-C lyase (PHL) catalyzing the reactionR-GlyOH.fwdarw.R-NH.sub.2wherein R represents a peptide residue, and GlyOH represents an .alpha.-hydroxyglycine residue linked to the C-terminus of said peptide R by an amide bond, a recombinant DNA molecule coding for a PHL, a method for the preparation of such a recombinant DNA molecule, processes for the preparation of PHL from a natural source or by means of the said recombinant DNA molecule, and the use of PHL for the preparation of an amidated peptide R-NH.sub.2. | ||||||
| 17 | COMPOSITIONS AND METHODS FOR IMPROVED PROTEIN PRODUCTION | US15503859 | 2015-08-14 | US20170233746A1 | 2017-08-17 | Susan M. MADRID |
| Aspects of the present disclosure are drawn to methods of improving the expression of secreted cuproenzymes from host cells by manipulating the expression level of one or more proteins involved in copper transport in the host cell, e.g., membrane-bound copper transporting ATPases and soluble copper transporters. The present disclosure also provides compositions containing such improved host cells as well as products derived from the improved host cells that contain one or more cuproenzymes of interest. | ||||||
| 18 | Reduction of formation of amidated amino acids in cell lines for protein expression | US14384803 | 2013-04-16 | US09637769B2 | 2017-05-02 | Mihaela {hacek over (S)}kulj; Dominik Gaser |
| The present invention is related to a method to reduce peptide amidation activity in a given cell line, cell lines with reduced peptide amidation activity, and uses thereof. | ||||||
| 19 | REDUCTION OF FORMATION OF AMIDATED AMINO ACIDS IN CELL LINES FOR PROTEIN EXPRESSION | US14384803 | 2013-04-16 | US20150079634A1 | 2015-03-19 | Mihaela Skulj; Dominik Gaser |
| The present invention is related to a method to reduce peptide amidation activity in a given cell line, cell lines with reduced peptide amidation activity, and uses thereof. | ||||||
| 20 | Signature Of Secreted Protein Isoforms Specific To Ovarian Cancer | US13128955 | 2010-04-14 | US20120122113A1 | 2012-05-17 | Panagiotis Prions; Julian Venables; Benoit Chabot; Sherif Abou Elela |
| The present invention relates to the identification of secreted protein isoforms specific in ovarian cancer and methods for diagnosis or prognosis of ovarian cancer in a subject by detecting the secreted protein isoforms. | ||||||
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