CS236487B2 - Method of heptadecapeptide preparation - Google Patents

Method of heptadecapeptide preparation Download PDF

Info

Publication number: CS236487B2
Authority: CS; Czechoslovakia
Prior art keywords: arg; heptadecapeptide; leu; lys; purified
Prior art date: 1981-07-21

Application number

CS825579A

Other languages

Czech (cs)

English (en)

Inventor

Shinro Tachibana

Kengo Araki

Shizuko Ohya

Seiji Yoshida

Original Assignee

Eisai 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.)

1981-07-21

Filing date

1982-07-21

Publication date

1985-05-15

1982-07-21 Application filed by Eisai Co Ltd filed Critical Eisai Co Ltd

1985-05-15 Publication of CS236487B2 publication Critical patent/CS236487B2/cs

Links

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Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/665—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans derived from pro-opiomelanocortin, pro-enkephalin or pro-dynorphin
- C07K14/675—Beta-endorphins
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/04—Centrally acting analgesics, e.g. opioids
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Gastroenterology & Hepatology (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Genetics & Genomics (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Zoology (AREA)
Toxicology (AREA)
Biomedical Technology (AREA)
Pain & Pain Management (AREA)
Neurosurgery (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Pharmacology & Pharmacy (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Neurology (AREA)
General Chemical & Material Sciences (AREA)
Animal Behavior & Ethology (AREA)
Chemical Kinetics & Catalysis (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

CS825579A 1981-07-21 1982-07-21 Method of heptadecapeptide preparation CS236487B2 (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP56112950A JPS5815946A (ja)	1981-07-21	1981-07-21	新規ヘプタデカペプタイド

Publications (1)

Publication Number	Publication Date
CS236487B2 true CS236487B2 (en)	1985-05-15

Family

ID=14599576

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CS825579A CS236487B2 (en)	1981-07-21	1982-07-21	Method of heptadecapeptide preparation

Country Status (8)

Country	Link
US (1)	US4481138A (da)
EP (1)	EP0070569B1 (da)
JP (1)	JPS5815946A (da)
CA (1)	CA1234565A (da)
CS (1)	CS236487B2 (da)
DE (1)	DE3264768D1 (da)
DK (1)	DK171680B1 (da)
HU (1)	HU186955B (da)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4462941A (en)	1982-06-10	1984-07-31	The Regents Of The University Of California	Dynorphin amide analogs
US4481191A (en) *	1983-03-30	1984-11-06	The Regents Of The University Of California	Method for controlling blood pressure
US5340802A (en) *	1989-06-30	1994-08-23	Abbott Laboratories	Peptide analog type-B CCK receptor ligands
EP4558004A1 (en)	2022-07-22	2025-05-28	The Gillette Company LLC	Personal care product dispensing system
USD1056337S1 (en)	2022-07-22	2024-12-31	The Gillette Company Llc	Shaving composition applicator

Family Cites Families (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US3013944A (en) *	1959-12-07	1961-12-19	Jorpes Johan Erik	Process for the production of gastrointestinal hormones and hormone concentrate
FR1605434A (da) *	1967-12-19	1975-10-17
DE2628006C2 (de) *	1976-06-23	1986-11-27	Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V., 3400 Göttingen	Tridecapeptid, Verfahren zu seiner Herstellung und seine Verwendung
HU175152B (hu) *	1976-12-30	1980-05-28	Richter Gedeon Vegyeszet	Sposob poluchenija peptidov s gastrin-aktivnost'ju, soderzhahhikh amino-oksi-kisloty
JPS6040412B2 (ja) *	1977-02-10	1985-09-11	エーザイ株式会社	消化管ホルモンの製造方法

1981
- 1981-07-21 JP JP56112950A patent/JPS5815946A/ja active Granted
1982
- 1982-07-20 HU HU822352A patent/HU186955B/hu not_active IP Right Cessation
- 1982-07-20 CA CA000407628A patent/CA1234565A/en not_active Expired
- 1982-07-20 DK DK326082A patent/DK171680B1/da active
- 1982-07-21 EP EP82106574A patent/EP0070569B1/en not_active Expired
- 1982-07-21 DE DE8282106574T patent/DE3264768D1/de not_active Expired
- 1982-07-21 CS CS825579A patent/CS236487B2/cs unknown
- 1982-07-21 US US06/400,324 patent/US4481138A/en not_active Expired - Lifetime

Also Published As

Publication number	Publication date
HU186955B (en)	1985-10-28
JPS5815946A (ja)	1983-01-29
JPH032880B2 (da)	1991-01-17
DK326082A (da)	1983-01-22
DK171680B1 (da)	1997-03-10
EP0070569B1 (en)	1985-07-17
EP0070569A1 (en)	1983-01-26
US4481138A (en)	1984-11-06
CA1234565A (en)	1988-03-29
DE3264768D1 (en)	1985-08-22

Publication	Publication Date	Title
Anastasi et al.	1972	Isolation and amino acid sequences of alytesin and bombesin, two analogous active tetradecapeptides from the skin of European discoglossid frogs
Montecucchi et al.	1980	Isolation and amino acid composition of sauvagine: an active polypeptide from methanol extracts of the skin of the South American frog Phyllomedusa sauvagei
Eysselein et al.	1982	Partial structure of a large canine cholecystokinin (CCK58): amino acid sequence
Fernandez et al.	1978	Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a.
Daly et al.	1992	Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor.
Said et al.	1972	Isolation from porcine‐intestinal wall of a vasoactive octacosapeptide related to secretin and to glucagon
Rossier et al.	1980	Met-enkephalin-Arg6-Phe7, present in high amounts in brain of rat, cattle and man, is an opioid agonist
Hansbrough et al.	1981	Speract. Purification and characterization of a peptide associated with eggs that activates spermatozoa.
Grandy et al.	1990	Purification, cloning, and tissue distribution of a 23-kDa rat protein isolated by morphine affinity chromatography
Carraway et al.	1980	Isolation, structure and biologic activity of chicken intestinal neurotensin
Nilsson	1974	Isolation, amino acid composition and terminal amino acid residues of the vasoactive octacosapeptide from chicken intestine. Partial purification of chicken secretin
EP0185034A1 (da)	1986-06-25
JPH01501148A (ja)	1989-04-20	悪性‐ＰＴＨｒＰの液性過カルシウム血症において活性なタンパク
JP2004532604A5 (da)	2010-10-21
Baumann et al.	1982	Purification and identification of neurohormone D, a heart accelerating peptide from the corpora cardiaca of the cockroach Periplaneta americana
JPH0822876B2 (ja)	1996-03-06	ペプチドホルモンカルジオジラチン及びその製造法
Price	1982	The FMRFamide-like peptide of Helix aspersa
CN105131084A (zh)	2015-12-09	基于内吗啡肽2或Biphalin的棕榈酰化修饰的阿片肽类似物及其合成和应用
Gregory et al.	1983	Isolation from porcine antral mucosa of a hexapeptide corresponding to the C-terminal sequence of gastrin
CS236487B2 (en)	1985-05-15	Method of heptadecapeptide preparation
Fukui et al.	1983	Isolation from bovine brain of a novel analgesic pentapeptide, neo-kyotorphin, containing the Tyr-Arg (kyotorphin) unit
AU640158B2 (en)	1993-08-19	Dynorphin analogs specific for kappa opioid receptors
Keller	1981	Purification and amino acid composition of the hyperglycemic neurohormone from the sinus gland of Orconectes limosus and comparison with the hormone from Carcinus maenas
US4632780A (en)	1986-12-30	N-terminal fragment of human pro-opiomelanocortin and process therefor
Greene et al.	1977	Isolation of myocardial depressant factor from plasma of dogs in hemorrhagic shock