Aminopeptidases in human retroplacental sera: Purification and characterization of two enzymes
Ten different maternal serum samples were analyzed for the hydrolysis of S-Bz-Cys-pNA (substrate for CAP) and Ala-pNA. The results showed clear differences in the activities in individual sera. Similar S-Bz-Cys-pNA hydrolysis activity was detected for all sera. However, Ala-pNA hydrolysis activity d...
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| Veröffentlicht in: | Biochemical medicine and metabolic biology 1989-04, Vol.41 (2), p.139-148 |
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| container_title | Biochemical medicine and metabolic biology |
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| creator | Watanabe, Yasuhiro Kumagai, Yuka Kubo, Yoshikazu Shimamori, Yoshimitsu Fujimoto, Yukio |
| description | Ten different maternal serum samples were analyzed for the hydrolysis of S-Bz-Cys-pNA (substrate for CAP) and Ala-pNA. The results showed clear differences in the activities in individual sera. Similar S-Bz-Cys-pNA hydrolysis activity was detected for all sera. However, Ala-pNA hydrolysis activity differed remarkably. Serum exhibiting low Ala-pNA hydrolysis activity contained only CAP, and that exhibiting high Ala-pNA hydrolyzing activity contained CAP and AAP. The two aminopeptidases were independently purified to a homogeneous state through the same purification procedures and some of their biochemical properties were compared. The enzymes were quite different with respect to molecular mass, the substrate specificities for some aminoacyl-pNA substrates, and the effects of inhibitors. Among various natural peptides tested for hydrolysis, the enzymes hydrolyzed Met-enkephalin most rapidly, but their modes of action were different. Furthermore, only CAP degraded oxytocin and AAP exhibited a high kinin-converting activity. |
| doi_str_mv | 10.1016/0885-4505(89)90019-4 |
| format | Article |
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The results showed clear differences in the activities in individual sera. Similar S-Bz-Cys-pNA hydrolysis activity was detected for all sera. However, Ala-pNA hydrolysis activity differed remarkably. Serum exhibiting low Ala-pNA hydrolysis activity contained only CAP, and that exhibiting high Ala-pNA hydrolyzing activity contained CAP and AAP. The two aminopeptidases were independently purified to a homogeneous state through the same purification procedures and some of their biochemical properties were compared. The enzymes were quite different with respect to molecular mass, the substrate specificities for some aminoacyl-pNA substrates, and the effects of inhibitors. Among various natural peptides tested for hydrolysis, the enzymes hydrolyzed Met-enkephalin most rapidly, but their modes of action were different. 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The results showed clear differences in the activities in individual sera. Similar S-Bz-Cys-pNA hydrolysis activity was detected for all sera. However, Ala-pNA hydrolysis activity differed remarkably. Serum exhibiting low Ala-pNA hydrolysis activity contained only CAP, and that exhibiting high Ala-pNA hydrolyzing activity contained CAP and AAP. The two aminopeptidases were independently purified to a homogeneous state through the same purification procedures and some of their biochemical properties were compared. The enzymes were quite different with respect to molecular mass, the substrate specificities for some aminoacyl-pNA substrates, and the effects of inhibitors. Among various natural peptides tested for hydrolysis, the enzymes hydrolyzed Met-enkephalin most rapidly, but their modes of action were different. Furthermore, only CAP degraded oxytocin and AAP exhibited a high kinin-converting activity.</description><subject>Aminopeptidases - analysis</subject><subject>Aminopeptidases - isolation & purification</subject><subject>Aminopeptidases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Hydrolysis</subject><subject>In Vitro Techniques</subject><subject>Molecular Weight</subject><subject>Peptides - analysis</subject><subject>Placenta - enzymology</subject><subject>Pregnancy</subject><subject>Proteins - metabolism</subject><issn>0885-4505</issn><issn>1557-7651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1rFTEUhoMo9bb6DxSyUepiNJkkk6QLoRS_oKAL3RoyyQmNzCRjklHaX-9c76XuXB0453lfDg9Czyh5TQkd3hClRMcFEedKv9KEUN3xB2hHhZCdHAR9iHb3yGN0WusPQohmgp-gk15SrYTeoe-Xc0x5gaVFbytUHBO-WWebcIFW8jJZB6nZCVco9gJ_WUsM0dkWc8I2eexubLGuQYl3h2UOuP3OGNLd7Qz1CXoU7FTh6XGeoW_v3329-thdf_7w6eryunOM9K2TfGSWcxWsCMxLEogLUhA1Kk09V94pHaiTw9hbPfqhd0IwrXvKiOcAwbMz9PLQu5T8c4XazByrg2myCfJajdz8MEXpBvID6EqutUAwS4mzLbeGErPXavbOzN6ZUdr81Wr4Fnt-7F_HGfx96Ohxu7843m11dgrFJhfrv27N9CDVsHFvDxxsMn5FKKa6CMmBjwVcMz7H_z_yBwXOlX8</recordid><startdate>198904</startdate><enddate>198904</enddate><creator>Watanabe, Yasuhiro</creator><creator>Kumagai, Yuka</creator><creator>Kubo, Yoshikazu</creator><creator>Shimamori, Yoshimitsu</creator><creator>Fujimoto, Yukio</creator><general>Elsevier Inc</general><general>Academic Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>198904</creationdate><title>Aminopeptidases in human retroplacental sera: Purification and characterization of two enzymes</title><author>Watanabe, Yasuhiro ; Kumagai, Yuka ; Kubo, Yoshikazu ; Shimamori, Yoshimitsu ; Fujimoto, Yukio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c302t-74b3a448fa5f3d70f0cf7508b891d48dc89f1c76b2a9bd62c553992130d4eefd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Aminopeptidases - analysis</topic><topic>Aminopeptidases - isolation & purification</topic><topic>Aminopeptidases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Hydrolysis</topic><topic>In Vitro Techniques</topic><topic>Molecular Weight</topic><topic>Peptides - analysis</topic><topic>Placenta - enzymology</topic><topic>Pregnancy</topic><topic>Proteins - metabolism</topic><toplevel>online_resources</toplevel><creatorcontrib>Watanabe, Yasuhiro</creatorcontrib><creatorcontrib>Kumagai, Yuka</creatorcontrib><creatorcontrib>Kubo, Yoshikazu</creatorcontrib><creatorcontrib>Shimamori, Yoshimitsu</creatorcontrib><creatorcontrib>Fujimoto, Yukio</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical medicine and metabolic biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watanabe, Yasuhiro</au><au>Kumagai, Yuka</au><au>Kubo, Yoshikazu</au><au>Shimamori, Yoshimitsu</au><au>Fujimoto, Yukio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aminopeptidases in human retroplacental sera: Purification and characterization of two enzymes</atitle><jtitle>Biochemical medicine and metabolic biology</jtitle><addtitle>Biochem Med Metab Biol</addtitle><date>1989-04</date><risdate>1989</risdate><volume>41</volume><issue>2</issue><spage>139</spage><epage>148</epage><pages>139-148</pages><issn>0885-4505</issn><eissn>1557-7651</eissn><coden>BMMBES</coden><abstract>Ten different maternal serum samples were analyzed for the hydrolysis of S-Bz-Cys-pNA (substrate for CAP) and Ala-pNA. The results showed clear differences in the activities in individual sera. Similar S-Bz-Cys-pNA hydrolysis activity was detected for all sera. However, Ala-pNA hydrolysis activity differed remarkably. Serum exhibiting low Ala-pNA hydrolysis activity contained only CAP, and that exhibiting high Ala-pNA hydrolyzing activity contained CAP and AAP. The two aminopeptidases were independently purified to a homogeneous state through the same purification procedures and some of their biochemical properties were compared. The enzymes were quite different with respect to molecular mass, the substrate specificities for some aminoacyl-pNA substrates, and the effects of inhibitors. Among various natural peptides tested for hydrolysis, the enzymes hydrolyzed Met-enkephalin most rapidly, but their modes of action were different. 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| ispartof | Biochemical medicine and metabolic biology, 1989-04, Vol.41 (2), p.139-148 |
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| subjects | Aminopeptidases - analysis Aminopeptidases - isolation & purification Aminopeptidases - metabolism Analytical, structural and metabolic biochemistry Biological and medical sciences Chromatography, DEAE-Cellulose Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Female Fundamental and applied biological sciences. Psychology Humans Hydrolases Hydrolysis In Vitro Techniques Molecular Weight Peptides - analysis Placenta - enzymology Pregnancy Proteins - metabolism |
| title | Aminopeptidases in human retroplacental sera: Purification and characterization of two enzymes |
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