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Use of New Synthetic Substrates for Assays of Cathepsin L and Cathepsin B

Efficient methods were developed for synthesizing synthetic substrates for assays of cathepsin B and cathepsin L. Several 2-naphthylamide compounds with a blocked NH2-terminus Suc-Tyr-Met-NA, β-Ala-Tyr-Met-NA, and D-Leu-Tyr-Met NA, were specific and sensitive substrates for cathepsin L and cathepsin...

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Published in:	Journal of biochemistry (Tokyo) 1983-01, Vol.93 (4), p.1129-1135
Main Authors:	KATUNUMA, Nobuhiko, TOWATARI, Takae, TAMAI, Masaharu, HANADA, Kazunori
Format:	Article
Language:	English
Subjects:	Analytical, structural and metabolic biochemistry Animals assays Biological and medical sciences Cathepsin B Cathepsin L Cathepsins - analysis Cysteine Endopeptidases Endopeptidases Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases Hydrolysis Male Rats Rats, Inbred Strains Substrate Specificity
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container_end_page	1135
container_issue	4
container_start_page	1129
container_title	Journal of biochemistry (Tokyo)
container_volume	93
creator	KATUNUMA, Nobuhiko TOWATARI, Takae TAMAI, Masaharu HANADA, Kazunori
description	Efficient methods were developed for synthesizing synthetic substrates for assays of cathepsin B and cathepsin L. Several 2-naphthylamide compounds with a blocked NH2-terminus Suc-Tyr-Met-NA, β-Ala-Tyr-Met-NA, and D-Leu-Tyr-Met NA, were specific and sensitive substrates for cathepsin L and cathepsin B; they were not specific for cathepsin L only, because all of them were also hydrolyzed by cathepsin B. Some kinetic constants for the hydrolyses of these three synthetic substrates by cathepsin B and cathepsin L are given.
doi_str_mv	10.1093/oxfordjournals.jbchem.a134238
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Several 2-naphthylamide compounds with a blocked NH2-terminus Suc-Tyr-Met-NA, β-Ala-Tyr-Met-NA, and D-Leu-Tyr-Met NA, were specific and sensitive substrates for cathepsin L and cathepsin B; they were not specific for cathepsin L only, because all of them were also hydrolyzed by cathepsin B. 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Several 2-naphthylamide compounds with a blocked NH2-terminus Suc-Tyr-Met-NA, β-Ala-Tyr-Met-NA, and D-Leu-Tyr-Met NA, were specific and sensitive substrates for cathepsin L and cathepsin B; they were not specific for cathepsin L only, because all of them were also hydrolyzed by cathepsin B. Some kinetic constants for the hydrolyses of these three synthetic substrates by cathepsin B and cathepsin L are given.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>assays</subject><subject>Biological and medical sciences</subject><subject>Cathepsin B</subject><subject>Cathepsin L</subject><subject>Cathepsins - analysis</subject><subject>Cysteine Endopeptidases</subject><subject>Endopeptidases</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>Hydrolysis</subject><subject>Male</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Substrate Specificity</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNqF0E1Lw0AQBuBFlFqrP0HIQb2lZr-zxxqsLRYVarV4WTabDU3NR91NsP33phiKN0_D8D7MDAPANQyGMBD4ttqmlU3WVWNLlbvhOtYrUwwVxATh8Aj0IafMR4zCY9APAgR9gcjyFJw5t963COMe6LGQYYRpH0wXznhV6j2Zb2--K-uVqTPtzZvY1VbVxnntMm_knNq5PYtUKzYuK72Zp8rkT393Dk7S9iBz0dUBWIzvX6OJP3t-mEajmZ8RKmqfsFgzrUicEM5VwgnkmkMap5ok2iAqEsYER0LTVCARKoh4oE2IIEecKMrxANz8zt3Y6qsxrpZF5rTJc1WaqnEyDChikIt_IcRUhK1u4WUHm7gwidzYrFB2J7sntflVlyunVZ5aVerMHZhgECNEWub_sszVZnuIlf2UjGNO5WT5Id-il_nj-B1LgX8AtkqKEA</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>KATUNUMA, Nobuhiko</creator><creator>TOWATARI, Takae</creator><creator>TAMAI, Masaharu</creator><creator>HANADA, Kazunori</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19830101</creationdate><title>Use of New Synthetic Substrates for Assays of Cathepsin L and Cathepsin B</title><author>KATUNUMA, Nobuhiko ; TOWATARI, Takae ; TAMAI, Masaharu ; HANADA, Kazunori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i459t-46bc6ca4bd477ad7417c715bfc4dce259d669729c5f9298a1270ce8217274a573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>assays</topic><topic>Biological and medical sciences</topic><topic>Cathepsin B</topic><topic>Cathepsin L</topic><topic>Cathepsins - analysis</topic><topic>Cysteine Endopeptidases</topic><topic>Endopeptidases</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases</topic><topic>Hydrolysis</topic><topic>Male</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KATUNUMA, Nobuhiko</creatorcontrib><creatorcontrib>TOWATARI, Takae</creatorcontrib><creatorcontrib>TAMAI, Masaharu</creatorcontrib><creatorcontrib>HANADA, Kazunori</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KATUNUMA, Nobuhiko</au><au>TOWATARI, Takae</au><au>TAMAI, Masaharu</au><au>HANADA, Kazunori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Use of New Synthetic Substrates for Assays of Cathepsin L and Cathepsin B</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>93</volume><issue>4</issue><spage>1129</spage><epage>1135</epage><pages>1129-1135</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Efficient methods were developed for synthesizing synthetic substrates for assays of cathepsin B and cathepsin L. 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source	J-STAGE Freely Available Titles - English; Oxford University Press Archive
subjects	Analytical, structural and metabolic biochemistry Animals assays Biological and medical sciences Cathepsin B Cathepsin L Cathepsins - analysis Cysteine Endopeptidases Endopeptidases Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases Hydrolysis Male Rats Rats, Inbred Strains Substrate Specificity
title	Use of New Synthetic Substrates for Assays of Cathepsin L and Cathepsin B
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