purification method for specific serine proteases using one-step affinity chromatography
A simple affinity chromatography procedure for specific isolation of serine proteases is described. The procedure was tested using enzymes from five microbial and one plant source. Feather keratin, covalently bound to controlled‐pore glass, was the support and magnesium chloride was used in the elut...
Gespeichert in:
| Veröffentlicht in: | Journal of chemical technology and biotechnology (1986) 1994-06, Vol.60 (2), p.153-160 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 160 |
|---|---|
| container_issue | 2 |
| container_start_page | 153 |
| container_title | Journal of chemical technology and biotechnology (1986) |
| container_volume | 60 |
| creator | Grzywnowicz, K Lobarzewski, J |
| description | A simple affinity chromatography procedure for specific isolation of serine proteases is described. The procedure was tested using enzymes from five microbial and one plant source. Feather keratin, covalently bound to controlled‐pore glass, was the support and magnesium chloride was used in the elution buffers instead of zinc chloride. This enabled one‐step isolation of serine proteases present in the biological materials used. The small (15 cm × 1 cm) controlled‐pore keratin‐glass column allowed high flow rates and protected the proteases from autodigestion during the chromatography process. The serine proteases were eluted from the column with good recovery (40–84·6%) and a purification efficiency between 5 and 7. The purified proteases were homogeneous by polyacrylamide gel electrophoresis. |
| doi_str_mv | 10.1002/jctb.280600207 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_26558117</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>26558117</sourcerecordid><originalsourceid>FETCH-LOGICAL-c390t-7936b2ec5dd6bec38134a72b9e37973fba0cac3aabf80fa83b84de899815f7b43</originalsourceid><addsrcrecordid>eNqFkM1vEzEUxC0EEqFw7RUfELcNz_auP44QoEVq6aFU7c1669iJS7Le2o5E_vtulCpXTk9P85vRaAg5ZzBnAPzLo6v9nGuQ0wPqFZkxMKpppYTXZAZc6oZ3qntL3pXyCABSczkjD-MuxxAd1pgGuvV1nZY0pEzL6N1BoMXnOHg65lQ9Fl_orsRhRdPgm1L9SDGEOMS6p26d0xZrWmUc1_v35E3ATfEfXu4Zufv548_isrm6ufi1-HrVOGGgNsoI2XPvuuVS9t4JzUSLivfGC2WUCD2CQycQ-6AhoBa9bpdeG6NZF1TfijPy-Zg7FXza-VLtNhbnNxscfNoVy2XXacbUf0EmDWfGwATOj6DLqZTsgx1z3GLeWwb2sLQ9LG1PS0-GTy_JWBxuQsbBxXJytVOy1IemzRGL027_TjLmv1YqoTp7__vCdt-v9eLhm7DXE__xyAdMFld5iry75cAEsNZAy0E8AzrpmMU</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16921990</pqid></control><display><type>article</type><title>purification method for specific serine proteases using one-step affinity chromatography</title><source>Wiley Journals</source><creator>Grzywnowicz, K ; Lobarzewski, J</creator><creatorcontrib>Grzywnowicz, K ; Lobarzewski, J</creatorcontrib><description>A simple affinity chromatography procedure for specific isolation of serine proteases is described. The procedure was tested using enzymes from five microbial and one plant source. Feather keratin, covalently bound to controlled‐pore glass, was the support and magnesium chloride was used in the elution buffers instead of zinc chloride. This enabled one‐step isolation of serine proteases present in the biological materials used. The small (15 cm × 1 cm) controlled‐pore keratin‐glass column allowed high flow rates and protected the proteases from autodigestion during the chromatography process. The serine proteases were eluted from the column with good recovery (40–84·6%) and a purification efficiency between 5 and 7. The purified proteases were homogeneous by polyacrylamide gel electrophoresis.</description><identifier>ISSN: 0268-2575</identifier><identifier>EISSN: 1097-4660</identifier><identifier>DOI: 10.1002/jctb.280600207</identifier><identifier>CODEN: JCTBDC</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>affinity chromatography ; Biological and medical sciences ; Biotechnology ; Brassica oleracea var. capitata ; chromatography ; Coriolus versicolor ; enzyme activity ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; Improved methods for extraction and purification of enzymes ; keratin ; keratin ligand ; Methods. Procedures. Technologies ; Phlebia ; phlebia radiata ; purification ; serine proteases ; serine proteinases ; trichophyton gallinae ; Trichophyton verrucosum</subject><ispartof>Journal of chemical technology and biotechnology (1986), 1994-06, Vol.60 (2), p.153-160</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-7936b2ec5dd6bec38134a72b9e37973fba0cac3aabf80fa83b84de899815f7b43</citedby><cites>FETCH-LOGICAL-c390t-7936b2ec5dd6bec38134a72b9e37973fba0cac3aabf80fa83b84de899815f7b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4169684$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Grzywnowicz, K</creatorcontrib><creatorcontrib>Lobarzewski, J</creatorcontrib><title>purification method for specific serine proteases using one-step affinity chromatography</title><title>Journal of chemical technology and biotechnology (1986)</title><addtitle>J. Chem. Technol. Biotechnol</addtitle><description>A simple affinity chromatography procedure for specific isolation of serine proteases is described. The procedure was tested using enzymes from five microbial and one plant source. Feather keratin, covalently bound to controlled‐pore glass, was the support and magnesium chloride was used in the elution buffers instead of zinc chloride. This enabled one‐step isolation of serine proteases present in the biological materials used. The small (15 cm × 1 cm) controlled‐pore keratin‐glass column allowed high flow rates and protected the proteases from autodigestion during the chromatography process. The serine proteases were eluted from the column with good recovery (40–84·6%) and a purification efficiency between 5 and 7. The purified proteases were homogeneous by polyacrylamide gel electrophoresis.</description><subject>affinity chromatography</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Brassica oleracea var. capitata</subject><subject>chromatography</subject><subject>Coriolus versicolor</subject><subject>enzyme activity</subject><subject>Enzyme engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Improved methods for extraction and purification of enzymes</subject><subject>keratin</subject><subject>keratin ligand</subject><subject>Methods. Procedures. Technologies</subject><subject>Phlebia</subject><subject>phlebia radiata</subject><subject>purification</subject><subject>serine proteases</subject><subject>serine proteinases</subject><subject>trichophyton gallinae</subject><subject>Trichophyton verrucosum</subject><issn>0268-2575</issn><issn>1097-4660</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNqFkM1vEzEUxC0EEqFw7RUfELcNz_auP44QoEVq6aFU7c1669iJS7Le2o5E_vtulCpXTk9P85vRaAg5ZzBnAPzLo6v9nGuQ0wPqFZkxMKpppYTXZAZc6oZ3qntL3pXyCABSczkjD-MuxxAd1pgGuvV1nZY0pEzL6N1BoMXnOHg65lQ9Fl_orsRhRdPgm1L9SDGEOMS6p26d0xZrWmUc1_v35E3ATfEfXu4Zufv548_isrm6ufi1-HrVOGGgNsoI2XPvuuVS9t4JzUSLivfGC2WUCD2CQycQ-6AhoBa9bpdeG6NZF1TfijPy-Zg7FXza-VLtNhbnNxscfNoVy2XXacbUf0EmDWfGwATOj6DLqZTsgx1z3GLeWwb2sLQ9LG1PS0-GTy_JWBxuQsbBxXJytVOy1IemzRGL027_TjLmv1YqoTp7__vCdt-v9eLhm7DXE__xyAdMFld5iry75cAEsNZAy0E8AzrpmMU</recordid><startdate>19940601</startdate><enddate>19940601</enddate><creator>Grzywnowicz, K</creator><creator>Lobarzewski, J</creator><general>John Wiley & Sons, Ltd</general><general>Wiley</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>F28</scope></search><sort><creationdate>19940601</creationdate><title>purification method for specific serine proteases using one-step affinity chromatography</title><author>Grzywnowicz, K ; Lobarzewski, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-7936b2ec5dd6bec38134a72b9e37973fba0cac3aabf80fa83b84de899815f7b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>affinity chromatography</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Brassica oleracea var. capitata</topic><topic>chromatography</topic><topic>Coriolus versicolor</topic><topic>enzyme activity</topic><topic>Enzyme engineering</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Improved methods for extraction and purification of enzymes</topic><topic>keratin</topic><topic>keratin ligand</topic><topic>Methods. Procedures. Technologies</topic><topic>Phlebia</topic><topic>phlebia radiata</topic><topic>purification</topic><topic>serine proteases</topic><topic>serine proteinases</topic><topic>trichophyton gallinae</topic><topic>Trichophyton verrucosum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grzywnowicz, K</creatorcontrib><creatorcontrib>Lobarzewski, J</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><jtitle>Journal of chemical technology and biotechnology (1986)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Grzywnowicz, K</au><au>Lobarzewski, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>purification method for specific serine proteases using one-step affinity chromatography</atitle><jtitle>Journal of chemical technology and biotechnology (1986)</jtitle><addtitle>J. Chem. Technol. Biotechnol</addtitle><date>1994-06-01</date><risdate>1994</risdate><volume>60</volume><issue>2</issue><spage>153</spage><epage>160</epage><pages>153-160</pages><issn>0268-2575</issn><eissn>1097-4660</eissn><coden>JCTBDC</coden><abstract>A simple affinity chromatography procedure for specific isolation of serine proteases is described. The procedure was tested using enzymes from five microbial and one plant source. Feather keratin, covalently bound to controlled‐pore glass, was the support and magnesium chloride was used in the elution buffers instead of zinc chloride. This enabled one‐step isolation of serine proteases present in the biological materials used. The small (15 cm × 1 cm) controlled‐pore keratin‐glass column allowed high flow rates and protected the proteases from autodigestion during the chromatography process. The serine proteases were eluted from the column with good recovery (40–84·6%) and a purification efficiency between 5 and 7. The purified proteases were homogeneous by polyacrylamide gel electrophoresis.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><doi>10.1002/jctb.280600207</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0268-2575 |
| ispartof | Journal of chemical technology and biotechnology (1986), 1994-06, Vol.60 (2), p.153-160 |
| issn | 0268-2575 1097-4660 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_26558117 |
| source | Wiley Journals |
| subjects | affinity chromatography Biological and medical sciences Biotechnology Brassica oleracea var. capitata chromatography Coriolus versicolor enzyme activity Enzyme engineering Fundamental and applied biological sciences. Psychology Improved methods for extraction and purification of enzymes keratin keratin ligand Methods. Procedures. Technologies Phlebia phlebia radiata purification serine proteases serine proteinases trichophyton gallinae Trichophyton verrucosum |
| title | purification method for specific serine proteases using one-step affinity chromatography |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T03%3A57%3A29IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=purification%20method%20for%20specific%20serine%20proteases%20using%20one-step%20affinity%20chromatography&rft.jtitle=Journal%20of%20chemical%20technology%20and%20biotechnology%20(1986)&rft.au=Grzywnowicz,%20K&rft.date=1994-06-01&rft.volume=60&rft.issue=2&rft.spage=153&rft.epage=160&rft.pages=153-160&rft.issn=0268-2575&rft.eissn=1097-4660&rft.coden=JCTBDC&rft_id=info:doi/10.1002/jctb.280600207&rft_dat=%3Cproquest_cross%3E26558117%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16921990&rft_id=info:pmid/&rfr_iscdi=true |