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Effects of Native and Denatured Whey Proteins on Plasminogen Activator Activity
The plasmin system native to bovine milk consists of the caseinolytic serine proteinase plasmin; its inactive zymogen, plasminogen; plasminogen activators; and inhibitors. Evidence in the literature indicates that whey proteins may inhibit plasmin activity, but there is very little mention of their...
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| Published in: | Journal of dairy science 2004-08, Vol.87 (8), p.2344-2350 |
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| container_title | Journal of dairy science |
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| creator | Rippel, K.M. Nielsen, S.S. Hayes, K.D. |
| description | The plasmin system native to bovine milk consists of the caseinolytic serine proteinase plasmin; its inactive zymogen, plasminogen; plasminogen activators; and inhibitors. Evidence in the literature indicates that whey proteins may inhibit plasmin activity, but there is very little mention of their effect on plasminogen activators. The objective of this research was to determine the effect of both unheated and heat-denatured β-lactoglobulin (β-LG), α-lactalbumin (α-LA), and BSA on plasminogen activators.
Plasminogen activator activity was significantly stimulated by non-heat treated and denatured α-LA as well as by denatured β-LG. The stimulation effect by these whey proteins was kinetically characterized, which showed that all 3 significantly increased the rate of plasminogen activation. The stimulation effect was shown to be independent of any effect of the whey proteins on plasmin activity by testing 2 different substrates, d-Val-Leu-Lys p-nitroanilide (S-2251) and Spectrozyme PL (Spec PL), in a plasmin assay. Results using S-2251 confirmed the inhibitory effect of whey proteins on plasmin observed by several researchers. However, use of SpecPL did not suggest inhibition. Ligand binding studies showed this discrepancy to be due to significant interaction between S-2251 and the whey proteins. Overall, this study indicates that whey protein incorporation into cheese may not hinder plasmin activity and may stimulate plasminogen activation. Furthermore, the results indicate the need for careful consideration of the type of synthetic substrate chosen for model work involving whey proteins and the plasmin system. |
| doi_str_mv | 10.3168/jds.S0022-0302(04)73356-1 |
| format | article |
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Plasminogen activator activity was significantly stimulated by non-heat treated and denatured α-LA as well as by denatured β-LG. The stimulation effect by these whey proteins was kinetically characterized, which showed that all 3 significantly increased the rate of plasminogen activation. The stimulation effect was shown to be independent of any effect of the whey proteins on plasmin activity by testing 2 different substrates, d-Val-Leu-Lys p-nitroanilide (S-2251) and Spectrozyme PL (Spec PL), in a plasmin assay. Results using S-2251 confirmed the inhibitory effect of whey proteins on plasmin observed by several researchers. However, use of SpecPL did not suggest inhibition. Ligand binding studies showed this discrepancy to be due to significant interaction between S-2251 and the whey proteins. Overall, this study indicates that whey protein incorporation into cheese may not hinder plasmin activity and may stimulate plasminogen activation. Furthermore, the results indicate the need for careful consideration of the type of synthetic substrate chosen for model work involving whey proteins and the plasmin system.</description><identifier>ISSN: 0022-0302</identifier><identifier>EISSN: 1525-3198</identifier><identifier>DOI: 10.3168/jds.S0022-0302(04)73356-1</identifier><identifier>PMID: 15328255</identifier><identifier>CODEN: JDSCAE</identifier><language>eng</language><publisher>Savoy, IL: Elsevier Inc</publisher><subject>Animal productions ; assays ; Biological and medical sciences ; bovine serum albumin ; denaturation ; enzyme activity ; enzyme inhibition ; enzyme kinetics ; enzyme substrates ; Fibrinolysin - metabolism ; Food industries ; Fundamental and applied biological sciences. Psychology ; Hot Temperature ; Kinetics ; lactalbumin ; Lactalbumin - pharmacology ; lactoglobulins ; Lactoglobulins - pharmacology ; Milk and cheese industries. Ice creams ; Milk Proteins - chemistry ; Milk Proteins - pharmacology ; Oligopeptides - metabolism ; plasmin ; Plasminogen - metabolism ; plasminogen activator ; Plasminogen Activators - metabolism ; protein degradation ; Protein Denaturation ; Structure-Activity Relationship ; substrate specificity ; Terrestrial animal productions ; Vertebrates ; whey protein ; Whey Proteins</subject><ispartof>Journal of dairy science, 2004-08, Vol.87 (8), p.2344-2350</ispartof><rights>2004 American Dairy Science Association</rights><rights>2004 INIST-CNRS</rights><rights>Copyright American Dairy Science Association Aug 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-30dc87593f935899a7e4cae9fb1e2326d1d38cfab9504615f9a0be8ab590ef483</citedby><cites>FETCH-LOGICAL-c536t-30dc87593f935899a7e4cae9fb1e2326d1d38cfab9504615f9a0be8ab590ef483</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15980556$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15328255$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rippel, K.M.</creatorcontrib><creatorcontrib>Nielsen, S.S.</creatorcontrib><creatorcontrib>Hayes, K.D.</creatorcontrib><title>Effects of Native and Denatured Whey Proteins on Plasminogen Activator Activity</title><title>Journal of dairy science</title><addtitle>J Dairy Sci</addtitle><description>The plasmin system native to bovine milk consists of the caseinolytic serine proteinase plasmin; its inactive zymogen, plasminogen; plasminogen activators; and inhibitors. Evidence in the literature indicates that whey proteins may inhibit plasmin activity, but there is very little mention of their effect on plasminogen activators. The objective of this research was to determine the effect of both unheated and heat-denatured β-lactoglobulin (β-LG), α-lactalbumin (α-LA), and BSA on plasminogen activators.
Plasminogen activator activity was significantly stimulated by non-heat treated and denatured α-LA as well as by denatured β-LG. The stimulation effect by these whey proteins was kinetically characterized, which showed that all 3 significantly increased the rate of plasminogen activation. The stimulation effect was shown to be independent of any effect of the whey proteins on plasmin activity by testing 2 different substrates, d-Val-Leu-Lys p-nitroanilide (S-2251) and Spectrozyme PL (Spec PL), in a plasmin assay. Results using S-2251 confirmed the inhibitory effect of whey proteins on plasmin observed by several researchers. However, use of SpecPL did not suggest inhibition. Ligand binding studies showed this discrepancy to be due to significant interaction between S-2251 and the whey proteins. Overall, this study indicates that whey protein incorporation into cheese may not hinder plasmin activity and may stimulate plasminogen activation. Furthermore, the results indicate the need for careful consideration of the type of synthetic substrate chosen for model work involving whey proteins and the plasmin system.</description><subject>Animal productions</subject><subject>assays</subject><subject>Biological and medical sciences</subject><subject>bovine serum albumin</subject><subject>denaturation</subject><subject>enzyme activity</subject><subject>enzyme inhibition</subject><subject>enzyme kinetics</subject><subject>enzyme substrates</subject><subject>Fibrinolysin - metabolism</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hot Temperature</subject><subject>Kinetics</subject><subject>lactalbumin</subject><subject>Lactalbumin - pharmacology</subject><subject>lactoglobulins</subject><subject>Lactoglobulins - pharmacology</subject><subject>Milk and cheese industries. Ice creams</subject><subject>Milk Proteins - chemistry</subject><subject>Milk Proteins - pharmacology</subject><subject>Oligopeptides - metabolism</subject><subject>plasmin</subject><subject>Plasminogen - metabolism</subject><subject>plasminogen activator</subject><subject>Plasminogen Activators - metabolism</subject><subject>protein degradation</subject><subject>Protein Denaturation</subject><subject>Structure-Activity Relationship</subject><subject>substrate specificity</subject><subject>Terrestrial animal productions</subject><subject>Vertebrates</subject><subject>whey protein</subject><subject>Whey Proteins</subject><issn>0022-0302</issn><issn>1525-3198</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqNkU1v1DAQhi0EokvhL0BAAsEhxZ9Z-1gt5UOqaKVScbS8znjXq8Ru7aRo_z1Os6KIEyfb0jPvzDxG6DXBJ4w08uOuzSdXGFNaY4bpe8w_LBkTTU0eoQURVNSMKPkYLf4gR-hZzrvyJBSLp-iICEYlFWKBLs6cAzvkKrrquxn8HVQmtNUnCGYYE7TVzy3sq8sUB_ChUKG67EzufYgbCNWpLRVmiGm--WH_HD1xpsvw4nAeo-vPZz9WX-vziy_fVqfntRWsGWqGWyuXQjGnmJBKmSVwa0C5NQHKaNOSlknrzFoJzBsinDJ4DdKshcLguGTH6N2ce5Pi7Qh50L3PFrrOBIhj1k0jCecNL-Cbf8BdHFMos2mihKRUMFYgNUM2xZwTOH2TfG_SXhOsJ-W6KNf3yvXkU2Ou75VrUmpfHhqM6x7ah8qD4wK8PQAmW9O5ZIL1-S9OSSxE87DS1m-2v3wCnXvTdSWWTO3lUktNGZ9WejWDzkRtNqmEXV9RTBjGijOuJjurmYDyBXceks7WQ7DQllg76Db6_9jsNym5td0</recordid><startdate>20040801</startdate><enddate>20040801</enddate><creator>Rippel, K.M.</creator><creator>Nielsen, S.S.</creator><creator>Hayes, K.D.</creator><general>Elsevier Inc</general><general>Am Dairy Sci Assoc</general><general>American Dairy Science Association</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><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>3V.</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7S</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>S0X</scope><scope>7X8</scope></search><sort><creationdate>20040801</creationdate><title>Effects of Native and Denatured Whey Proteins on Plasminogen Activator Activity</title><author>Rippel, K.M. ; Nielsen, S.S. ; Hayes, K.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-30dc87593f935899a7e4cae9fb1e2326d1d38cfab9504615f9a0be8ab590ef483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animal productions</topic><topic>assays</topic><topic>Biological and medical sciences</topic><topic>bovine serum albumin</topic><topic>denaturation</topic><topic>enzyme activity</topic><topic>enzyme inhibition</topic><topic>enzyme kinetics</topic><topic>enzyme substrates</topic><topic>Fibrinolysin - metabolism</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hot Temperature</topic><topic>Kinetics</topic><topic>lactalbumin</topic><topic>Lactalbumin - pharmacology</topic><topic>lactoglobulins</topic><topic>Lactoglobulins - pharmacology</topic><topic>Milk and cheese industries. Ice creams</topic><topic>Milk Proteins - chemistry</topic><topic>Milk Proteins - pharmacology</topic><topic>Oligopeptides - metabolism</topic><topic>plasmin</topic><topic>Plasminogen - metabolism</topic><topic>plasminogen activator</topic><topic>Plasminogen Activators - metabolism</topic><topic>protein degradation</topic><topic>Protein Denaturation</topic><topic>Structure-Activity Relationship</topic><topic>substrate specificity</topic><topic>Terrestrial animal productions</topic><topic>Vertebrates</topic><topic>whey protein</topic><topic>Whey Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rippel, K.M.</creatorcontrib><creatorcontrib>Nielsen, S.S.</creatorcontrib><creatorcontrib>Hayes, K.D.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</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>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Agriculture & Environmental Science Database</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Engineering Database</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of dairy science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rippel, K.M.</au><au>Nielsen, S.S.</au><au>Hayes, K.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of Native and Denatured Whey Proteins on Plasminogen Activator Activity</atitle><jtitle>Journal of dairy science</jtitle><addtitle>J Dairy Sci</addtitle><date>2004-08-01</date><risdate>2004</risdate><volume>87</volume><issue>8</issue><spage>2344</spage><epage>2350</epage><pages>2344-2350</pages><issn>0022-0302</issn><eissn>1525-3198</eissn><coden>JDSCAE</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The plasmin system native to bovine milk consists of the caseinolytic serine proteinase plasmin; its inactive zymogen, plasminogen; plasminogen activators; and inhibitors. Evidence in the literature indicates that whey proteins may inhibit plasmin activity, but there is very little mention of their effect on plasminogen activators. The objective of this research was to determine the effect of both unheated and heat-denatured β-lactoglobulin (β-LG), α-lactalbumin (α-LA), and BSA on plasminogen activators.
Plasminogen activator activity was significantly stimulated by non-heat treated and denatured α-LA as well as by denatured β-LG. The stimulation effect by these whey proteins was kinetically characterized, which showed that all 3 significantly increased the rate of plasminogen activation. The stimulation effect was shown to be independent of any effect of the whey proteins on plasmin activity by testing 2 different substrates, d-Val-Leu-Lys p-nitroanilide (S-2251) and Spectrozyme PL (Spec PL), in a plasmin assay. Results using S-2251 confirmed the inhibitory effect of whey proteins on plasmin observed by several researchers. However, use of SpecPL did not suggest inhibition. Ligand binding studies showed this discrepancy to be due to significant interaction between S-2251 and the whey proteins. Overall, this study indicates that whey protein incorporation into cheese may not hinder plasmin activity and may stimulate plasminogen activation. Furthermore, the results indicate the need for careful consideration of the type of synthetic substrate chosen for model work involving whey proteins and the plasmin system.</abstract><cop>Savoy, IL</cop><pub>Elsevier Inc</pub><pmid>15328255</pmid><doi>10.3168/jds.S0022-0302(04)73356-1</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of dairy science, 2004-08, Vol.87 (8), p.2344-2350 |
| issn | 0022-0302 1525-3198 |
| language | eng |
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| source | EZB Electronic Journals Library |
| subjects | Animal productions assays Biological and medical sciences bovine serum albumin denaturation enzyme activity enzyme inhibition enzyme kinetics enzyme substrates Fibrinolysin - metabolism Food industries Fundamental and applied biological sciences. Psychology Hot Temperature Kinetics lactalbumin Lactalbumin - pharmacology lactoglobulins Lactoglobulins - pharmacology Milk and cheese industries. Ice creams Milk Proteins - chemistry Milk Proteins - pharmacology Oligopeptides - metabolism plasmin Plasminogen - metabolism plasminogen activator Plasminogen Activators - metabolism protein degradation Protein Denaturation Structure-Activity Relationship substrate specificity Terrestrial animal productions Vertebrates whey protein Whey Proteins |
| title | Effects of Native and Denatured Whey Proteins on Plasminogen Activator Activity |
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