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Leukotriene A4 Hydrolase from Guinea Pig Lung: The Presence of Two Catalytically Active Forms

Leukotriene A4 hydrolase was purified to apparent homogeneity from the guinea pig lung. The molecular weight was determined to be 70kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme exhibited two active forms with different pI values (5.7 and 5.4) depending on the presence...

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Published in:	Journal of biochemistry (Tokyo) 1989-02, Vol.105 (2), p.261-264
Main Authors:	Bito, Haruhiko, Ohishi, Nobuya, Miki, Ichiro, Minami, Michiko, Tanabe, Tadashi, Shimizu, Takao, Seyama, Yousuke
Format:	Article
Language:	English
Subjects:	Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Chromatography, Ion Exchange Enzymes and enzyme inhibitors Epoxide Hydrolases - analysis Epoxide Hydrolases - isolation & purification Epoxide Hydrolases - metabolism Female Fundamental and applied biological sciences. Psychology Guinea Pigs Hydrolases Isoelectric Focusing Lung - enzymology Male Molecular Weight Sulfhydryl Reagents
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container_title	Journal of biochemistry (Tokyo)
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creator	Bito, Haruhiko Ohishi, Nobuya Miki, Ichiro Minami, Michiko Tanabe, Tadashi Shimizu, Takao Seyama, Yousuke
description	Leukotriene A4 hydrolase was purified to apparent homogeneity from the guinea pig lung. The molecular weight was determined to be 70kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme exhibited two active forms with different pI values (5.7 and 5.4) depending on the presence or absence of SH-reducing reagents during purification procedures. No significant differences were observed between both forms of the enzyme as regards the catalytic properties. The N-terminal 20 amino acid sequence (PEVVDTXSLASPATVXRTKH) showed a 90% identity to the human enzyme with a constitutive substitution of IIe-3 and Ser-14 (human) by Val-3 and Thr-14 (guinea pig), respectively.
doi_str_mv	10.1093/oxfordjournals.jbchem.a122650
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The N-terminal 20 amino acid sequence (PEVVDTXSLASPATVXRTKH) showed a 90% identity to the human enzyme with a constitutive substitution of IIe-3 and Ser-14 (human) by Val-3 and Thr-14 (guinea pig), respectively.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a122650</identifier><identifier>PMID: 2722767</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Amino Acids - analysis ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Chromatography, Ion Exchange ; Enzymes and enzyme inhibitors ; Epoxide Hydrolases - analysis ; Epoxide Hydrolases - isolation & purification ; Epoxide Hydrolases - metabolism ; Female ; Fundamental and applied biological sciences. 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The molecular weight was determined to be 70kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme exhibited two active forms with different pI values (5.7 and 5.4) depending on the presence or absence of SH-reducing reagents during purification procedures. No significant differences were observed between both forms of the enzyme as regards the catalytic properties. The N-terminal 20 amino acid sequence (PEVVDTXSLASPATVXRTKH) showed a 90% identity to the human enzyme with a constitutive substitution of IIe-3 and Ser-14 (human) by Val-3 and Thr-14 (guinea pig), respectively.</description><subject>Amino Acids - analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Ion Exchange</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Epoxide Hydrolases - analysis</subject><subject>Epoxide Hydrolases - isolation & purification</subject><subject>Epoxide Hydrolases - metabolism</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Guinea Pigs</topic><topic>Hydrolases</topic><topic>Isoelectric Focusing</topic><topic>Lung - enzymology</topic><topic>Male</topic><topic>Molecular Weight</topic><topic>Sulfhydryl Reagents</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bito, Haruhiko</creatorcontrib><creatorcontrib>Ohishi, Nobuya</creatorcontrib><creatorcontrib>Miki, Ichiro</creatorcontrib><creatorcontrib>Minami, Michiko</creatorcontrib><creatorcontrib>Tanabe, Tadashi</creatorcontrib><creatorcontrib>Shimizu, Takao</creatorcontrib><creatorcontrib>Seyama, Yousuke</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>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bito, Haruhiko</au><au>Ohishi, Nobuya</au><au>Miki, Ichiro</au><au>Minami, Michiko</au><au>Tanabe, Tadashi</au><au>Shimizu, Takao</au><au>Seyama, Yousuke</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Leukotriene A4 Hydrolase from Guinea Pig Lung: The Presence of Two Catalytically Active Forms</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1989-02</date><risdate>1989</risdate><volume>105</volume><issue>2</issue><spage>261</spage><epage>264</epage><pages>261-264</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Leukotriene A4 hydrolase was purified to apparent homogeneity from the guinea pig lung. The molecular weight was determined to be 70kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme exhibited two active forms with different pI values (5.7 and 5.4) depending on the presence or absence of SH-reducing reagents during purification procedures. No significant differences were observed between both forms of the enzyme as regards the catalytic properties. The N-terminal 20 amino acid sequence (PEVVDTXSLASPATVXRTKH) showed a 90% identity to the human enzyme with a constitutive substitution of IIe-3 and Ser-14 (human) by Val-3 and Thr-14 (guinea pig), respectively.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>2722767</pmid><doi>10.1093/oxfordjournals.jbchem.a122650</doi><tpages>4</tpages></addata></record>
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source	J-STAGE (Japan Science & Technology Information Aggregator, Electronic) - Open Access English articles; Oxford University Press Archive
subjects	Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Chromatography, Ion Exchange Enzymes and enzyme inhibitors Epoxide Hydrolases - analysis Epoxide Hydrolases - isolation & purification Epoxide Hydrolases - metabolism Female Fundamental and applied biological sciences. Psychology Guinea Pigs Hydrolases Isoelectric Focusing Lung - enzymology Male Molecular Weight Sulfhydryl Reagents
title	Leukotriene A4 Hydrolase from Guinea Pig Lung: The Presence of Two Catalytically Active Forms
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