JPS5768785A - Activity enhancement of protease - Google Patents

Activity enhancement of protease

Info

Publication number
JPS5768785A
JPS5768785A JP14508380A JP14508380A JPS5768785A JP S5768785 A JPS5768785 A JP S5768785A JP 14508380 A JP14508380 A JP 14508380A JP 14508380 A JP14508380 A JP 14508380A JP S5768785 A JPS5768785 A JP S5768785A
Authority
JP
Japan
Prior art keywords
peptide bond
protease
formula
metal protease
methylamine
Prior art date
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
JP14508380A
Other languages
Japanese (ja)
Other versions
JPS638748B2 (en
Inventor
Kuniyo Inoue
Koji Seto
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.)
Sagami Chemical Research Institute
Tosoh Corp
Original Assignee
Sagami Chemical Research Institute
Toyo Soda Manufacturing 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.)
Filing date
Publication date
Application filed by Sagami Chemical Research Institute, Toyo Soda Manufacturing Co Ltd filed Critical Sagami Chemical Research Institute
Priority to JP14508380A priority Critical patent/JPS5768785A/en
Publication of JPS5768785A publication Critical patent/JPS5768785A/en
Publication of JPS638748B2 publication Critical patent/JPS638748B2/ja
Granted legal-status Critical Current

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  • Enzymes And Modification Thereof (AREA)

Abstract

PURPOSE: To In cutting a peptide bond or carrying out a formation reaction using a metal protease, to enhance the activity of metal protease, by using methylamine or methylenediamin.
CONSTITUTION: For example, in forming amino acids shown by the formulasIand II by the formation of a peptide bond between the amino acid shown by the formula I(Z is benzyloxycarbonyl; Asp is aspartic acid residue) and the amino acid shown by the formula II(X is phenylalanine, tryprophan, tyrosine, leucine, isoleucine residue; R is lower alkyl or amino) or by the cutting of peptide bond shown by the formula III(Z, Asp, X, and R are as shown before) through an enzymatic reaction using a metal protease in an aqueous medium, about 0.5W2.5 mole methylamine or methylenediamine per l aqueous medium is added to the reaction system.
COPYRIGHT: (C)1982,JPO&Japio
JP14508380A 1980-10-18 1980-10-18 Activity enhancement of protease Granted JPS5768785A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP14508380A JPS5768785A (en) 1980-10-18 1980-10-18 Activity enhancement of protease

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP14508380A JPS5768785A (en) 1980-10-18 1980-10-18 Activity enhancement of protease

Publications (2)

Publication Number Publication Date
JPS5768785A true JPS5768785A (en) 1982-04-27
JPS638748B2 JPS638748B2 (en) 1988-02-24

Family

ID=15376981

Family Applications (1)

Application Number Title Priority Date Filing Date
JP14508380A Granted JPS5768785A (en) 1980-10-18 1980-10-18 Activity enhancement of protease

Country Status (1)

Country Link
JP (1) JPS5768785A (en)

Also Published As

Publication number Publication date
JPS638748B2 (en) 1988-02-24

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