JPH01191683A - 新規なプロテアーゼ - Google Patents

新規なプロテアーゼ

Info

Publication number: JPH01191683A
Authority: JP; Japan
Prior art keywords: protease; amino acid; activity; basic amino; arg
Prior art date: 1988-01-27
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Granted

Application number

JP63016285A

Other languages

English (en)

Japanese (ja)

Other versions

JPH0578305B2 (cs

Inventor

Hiroaki Yamamoto

浩明山本

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

M&D Research Co Ltd

Original Assignee

M&D Research Co Ltd

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1988-01-27

Filing date

1988-01-27

Publication date

1989-08-01

1988-01-27 Application filed by M&D Research Co Ltd filed Critical M&D Research Co Ltd

1988-01-27 Priority to JP63016285A priority Critical patent/JPH01191683A/ja

1989-01-24 Priority to EP89101200A priority patent/EP0336056B1/en

1989-01-24 Priority to DE68922014T priority patent/DE68922014T2/de

1989-01-26 Priority to CA000589189A priority patent/CA1318872C/en

1989-01-26 Priority to US07/301,988 priority patent/US5053333A/en

1989-01-27 Priority to KR1019890000900A priority patent/KR930005454B1/ko

1989-08-01 Publication of JPH01191683A publication Critical patent/JPH01191683A/ja

1993-10-28 Publication of JPH0578305B2 publication Critical patent/JPH0578305B2/ja

Status Granted legal-status Critical Current

Links

108091005804 Peptidases Proteins 0.000 title claims abstract description 51
239000004365 Protease Substances 0.000 title claims abstract description 51
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 title claims abstract description 47
241000222068 Sporobolomyces <Sporidiobolaceae> Species 0.000 claims abstract description 15
239000000758 substrate Substances 0.000 claims abstract description 10
240000004808 Saccharomyces cerevisiae Species 0.000 claims abstract description 9
210000004899 c-terminal region Anatomy 0.000 claims abstract description 6
239000000126 substance Substances 0.000 claims abstract description 3
239000000872 buffer Substances 0.000 claims description 17
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 claims description 3
125000000539 amino acid group Chemical group 0.000 abstract description 32
239000007853 buffer solution Substances 0.000 abstract description 7
230000015572 biosynthetic process Effects 0.000 abstract description 3
102000004169 proteins and genes Human genes 0.000 abstract description 3
108090000623 proteins and genes Proteins 0.000 abstract description 3
239000003795 chemical substances by application Substances 0.000 abstract description 2
238000012258 culturing Methods 0.000 abstract description 2
238000003786 synthesis reaction Methods 0.000 abstract description 2
102400000107 C-terminal peptide Human genes 0.000 abstract 1
150000001875 compounds Chemical class 0.000 abstract 1
230000003301 hydrolyzing effect Effects 0.000 abstract 1
239000000463 material Substances 0.000 abstract 1
238000002360 preparation method Methods 0.000 abstract 1
230000000694 effects Effects 0.000 description 43
102000004190 Enzymes Human genes 0.000 description 15
108090000790 Enzymes Proteins 0.000 description 15
238000006243 chemical reaction Methods 0.000 description 11
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
238000010586 diagram Methods 0.000 description 9
238000010828 elution Methods 0.000 description 8
229920002684 Sepharose Polymers 0.000 description 7
210000004027 cell Anatomy 0.000 description 7
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 6
235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 6
230000001580 bacterial effect Effects 0.000 description 6
239000012528 membrane Substances 0.000 description 6
239000000243 solution Substances 0.000 description 6
238000002523 gelfiltration Methods 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
239000006228 supernatant Substances 0.000 description 5
239000004094 surface-active agent Substances 0.000 description 5
102000035195 Peptidases Human genes 0.000 description 4
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 4
229910052921 ammonium sulfate Inorganic materials 0.000 description 4
235000011130 ammonium sulphate Nutrition 0.000 description 4
VEXZGXHMUGYJMC-UHFFFAOYSA-N hydrochloric acid Substances Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
238000000034 method Methods 0.000 description 4
239000002244 precipitate Substances 0.000 description 4
238000000746 purification Methods 0.000 description 4
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
150000001413 amino acids Chemical class 0.000 description 3
239000001110 calcium chloride Substances 0.000 description 3
229910001628 calcium chloride Inorganic materials 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
GLNDAGDHSLMOKX-UHFFFAOYSA-N coumarin 120 Chemical compound C1=C(N)C=CC2=C1OC(=O)C=C2C GLNDAGDHSLMOKX-UHFFFAOYSA-N 0.000 description 3
238000010438 heat treatment Methods 0.000 description 3
239000003112 inhibitor Substances 0.000 description 3
238000001155 isoelectric focusing Methods 0.000 description 3
238000005259 measurement Methods 0.000 description 3
229910021645 metal ion Inorganic materials 0.000 description 3
206010062767 Hypophysitis Diseases 0.000 description 2
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
102000006437 Proprotein Convertases Human genes 0.000 description 2
108010044159 Proprotein Convertases Proteins 0.000 description 2
WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 description 2
239000011575 calcium Substances 0.000 description 2
230000002255 enzymatic effect Effects 0.000 description 2
SFNALCNOMXIBKG-UHFFFAOYSA-N ethylene glycol monododecyl ether Chemical compound CCCCCCCCCCCCOCCO SFNALCNOMXIBKG-UHFFFAOYSA-N 0.000 description 2
239000000284 extract Substances 0.000 description 2
108020001507 fusion proteins Proteins 0.000 description 2
102000037865 fusion proteins Human genes 0.000 description 2
210000003635 pituitary gland Anatomy 0.000 description 2
238000011084 recovery Methods 0.000 description 2
238000005406 washing Methods 0.000 description 2
239000007218 ym medium Substances 0.000 description 2
JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 2
YPLZVJKSYBUKBU-UHFFFAOYSA-N 3-amino-4-methylchromen-2-one Chemical compound C1=CC=CC2=C1OC(=O)C(N)=C2C YPLZVJKSYBUKBU-UHFFFAOYSA-N 0.000 description 1
NYZMKJHGHNWMNX-UHFFFAOYSA-N 4-methyl-2-oxochromene-7-carboxamide Chemical compound C1=C(C(N)=O)C=CC2=C1OC(=O)C=C2C NYZMKJHGHNWMNX-UHFFFAOYSA-N 0.000 description 1
102000035101 Aspartic proteases Human genes 0.000 description 1
108091005502 Aspartic proteases Proteins 0.000 description 1
108010023063 Bacto-peptone Proteins 0.000 description 1
239000005711 Benzoic acid Substances 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
KRHYYFGTRYWZRS-UHFFFAOYSA-M Fluoride anion Chemical compound [F-] KRHYYFGTRYWZRS-UHFFFAOYSA-M 0.000 description 1
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
108010026459 IRCM-serine protease 1 Proteins 0.000 description 1
229910021380 Manganese Chloride Inorganic materials 0.000 description 1
GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 1
229910021586 Nickel(II) chloride Inorganic materials 0.000 description 1
238000007011 Robinson annulation reaction Methods 0.000 description 1
108091006629 SLC13A2 Proteins 0.000 description 1
108010022999 Serine Proteases Proteins 0.000 description 1
102000012479 Serine Proteases Human genes 0.000 description 1
239000013504 Triton X-100 Substances 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
239000012190 activator Substances 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
235000010233 benzoic acid Nutrition 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
239000002738 chelating agent Substances 0.000 description 1
RCTYPNKXASFOBE-UHFFFAOYSA-M chloromercury Chemical compound [Hg]Cl RCTYPNKXASFOBE-UHFFFAOYSA-M 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
GVPFVAHMJGGAJG-UHFFFAOYSA-L cobalt dichloride Chemical compound [Cl-].[Cl-].[Co+2] GVPFVAHMJGGAJG-UHFFFAOYSA-L 0.000 description 1
239000012141 concentrate Substances 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
229910000365 copper sulfate Inorganic materials 0.000 description 1
ARUVKPQLZAKDPS-UHFFFAOYSA-L copper(II) sulfate Chemical compound [Cu+2].[O-][S+2]([O-])([O-])[O-] ARUVKPQLZAKDPS-UHFFFAOYSA-L 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
238000010494 dissociation reaction Methods 0.000 description 1
230000005593 dissociations Effects 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
230000005284 excitation Effects 0.000 description 1
239000011536 extraction buffer Substances 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
239000008103 glucose Substances 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
229910001385 heavy metal Inorganic materials 0.000 description 1
239000005556 hormone Substances 0.000 description 1
229940088597 hormone Drugs 0.000 description 1
239000005457 ice water Substances 0.000 description 1
238000011534 incubation Methods 0.000 description 1
239000000411 inducer Substances 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
239000007788 liquid Substances 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
239000011565 manganese chloride Substances 0.000 description 1
235000002867 manganese chloride Nutrition 0.000 description 1
229940099607 manganese chloride Drugs 0.000 description 1
238000000691 measurement method Methods 0.000 description 1
239000002609 medium Substances 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Substances 0.000 description 1
HOVAGTYPODGVJG-VEIUFWFVSA-N methyl alpha-D-mannoside Chemical compound CO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O HOVAGTYPODGVJG-VEIUFWFVSA-N 0.000 description 1
244000005700 microbiome Species 0.000 description 1
QMMRZOWCJAIUJA-UHFFFAOYSA-L nickel dichloride Chemical compound Cl[Ni]Cl QMMRZOWCJAIUJA-UHFFFAOYSA-L 0.000 description 1
230000035790 physiological processes and functions Effects 0.000 description 1
108090000765 processed proteins & peptides Proteins 0.000 description 1
230000007017 scission Effects 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000003756 stirring Methods 0.000 description 1
-1 t-Butoxycarbonyl Chemical group 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
238000005199 ultracentrifugation Methods 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1
239000011592 zinc chloride Substances 0.000 description 1
235000005074 zinc chloride Nutrition 0.000 description 1

Landscapes

Enzymes And Modification Thereof (AREA)

JP63016285A 1988-01-27 1988-01-27 新規なプロテアーゼ Granted JPH01191683A (ja)

Priority Applications (6)

Application Number	Priority Date	Filing Date	Title
JP63016285A JPH01191683A (ja)	1988-01-27	1988-01-27	新規なプロテアーゼ
EP89101200A EP0336056B1 (en)	1988-01-27	1989-01-24	Protease
DE68922014T DE68922014T2 (de)	1988-01-27	1989-01-24	Protease.
CA000589189A CA1318872C (en)	1988-01-27	1989-01-26	Protease
US07/301,988 US5053333A (en)	1988-01-27	1989-01-26	Protease
KR1019890000900A KR930005454B1 (ko)	1988-01-27	1989-01-27	포로테아제

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP63016285A JPH01191683A (ja)	1988-01-27	1988-01-27	新規なプロテアーゼ

Publications (2)

Publication Number	Publication Date
JPH01191683A true JPH01191683A (ja)	1989-08-01
JPH0578305B2 JPH0578305B2 (cs)	1993-10-28

Family

ID=11912279

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP63016285A Granted JPH01191683A (ja)	1988-01-27	1988-01-27	新規なプロテアーゼ

Country Status (1)

Country	Link
JP (1)	JPH01191683A (cs)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
WO1992006211A1 (en) *	1990-10-09	1992-04-16	M & D Research Co., Ltd.	Process for producing peptide or protein

1988
- 1988-01-27 JP JP63016285A patent/JPH01191683A/ja active Granted

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
WO1992006211A1 (en) *	1990-10-09	1992-04-16	M & D Research Co., Ltd.	Process for producing peptide or protein
US5506120A (en) *	1990-10-09	1996-04-09	M & D Research Co., Ltd.	Method of producing peptides or proteins as fusion proteins

Also Published As

Publication number	Publication date
JPH0578305B2 (cs)	1993-10-28

Publication	Publication Date	Title
CN1054159C (zh)	2000-07-05	蛋白质的分离
Blumentals et al.	1990	Characterization of sodium dodecyl sulfate-resistant proteolytic activity in the hyperthermophilic archaebacterium Pyrococcus furiosus
Nordwig et al.	1968	A collagenolytic enzyme from Aspergillus oryzae: purification and properties
Griffin et al.	1992	Isolation and characterization of an alkaline protease from the marine shipworm bacterium
Thibault et al.	1981	Tonin, an esteroprotease from rat submaxillary glands
Dostál et al.	2005	The precursor of secreted aspartic proteinase Sapp1p from Candida parapsilosis can be activated both autocatalytically and by a membrane-bound processing proteinase.
Roncari et al.	1976	[43] Thermophilic aminopeptidase I
Hofmann	1976	[49] Penicillocarboxypeptidases S-1 and S-2
EP0336056B1 (en)	1995-04-05	Protease
ODA et al.	1986	Purification and Characterization of Acid Proteinase C of Scytalidium Hgnicolum ATCC 24568
Fukasawa et al.	1988	Some properties of two proteinases from a luminous bacterium, Vibrio harveyi strain FLN-108
EP4289943A1 (en)	2023-12-13	Protein deamidating enzyme
JP3915983B2 (ja)	2007-05-16	プロテアーゼ、このプロテアーゼをコードするｄｎａ、プロテアーゼの製造方法
JPH05992B2 (cs)	1993-01-07
JPH01191683A (ja)	1989-08-01	新規なプロテアーゼ
US5369016A (en)	1994-11-29	Peptide amidase and the use thereof
Merkel et al.	1981	A dimeric, extracellular, heat-stable aminopeptidase produced by a marine pseudomonad
JP3518868B2 (ja)	2004-04-12	バシラスリケニフォーミス菌株から由来したアミノペプチダーゼ及び天然蛋白質の製造方法
JPH0249585A (ja)	1990-02-19	新規なプロテアーゼ
JP3463951B2 (ja)	2003-11-05	耐熱性ピログルタミルペプチダーゼ及びその遺伝子
JPWO1997049819A1 (ja)	1999-07-21	新規なアミノ末端保護基遊離酵素
JP3478410B2 (ja)	2003-12-15	超耐熱性プロテアソーム
JP2794371B2 (ja)	1998-09-03	アルカリプロテアーゼｋ−１６ｈ
JPH0244511B2 (ja)	1990-10-04	Tainetsuseiarukarikinzokupuroteaazeoyobisonoseizoho
Masaki et al.	1986	Purification and Some Properties of Achromobacter Protease la from Achromobacter lyticus M497-1