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A cysteine endopeptidase from barley malt which degrades hordein
A cysteine endopeptidase of M r 29 000 which we have named malt endopeptidase-1 (MEP-1) was purified to homogeneity from a four-day green malt of barley ( Hordeum vulgare cv Schooner). It consists of two main species of pl 4.2 and 4.3 has a pH optimum of 4.5 for the hydrolysis of hordein and account...
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| Published in: | Phytochemistry (Oxford) 1989, Vol.28 (12), p.3285-3290 |
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| Main Authors: | , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c389t-314c1a53f2ad7f94ac775e8ffbdf9e9b4b9a5b21581bb10e51d1208379f5ead13 |
| container_end_page | 3290 |
| container_issue | 12 |
| container_start_page | 3285 |
| container_title | Phytochemistry (Oxford) |
| container_volume | 28 |
| creator | Phillips, Hilary A. Wallace, William |
| description | A cysteine endopeptidase of
M
r
29 000 which we have named malt endopeptidase-1 (MEP-1) was purified to homogeneity from a four-day green malt of barley (
Hordeum vulgare cv Schooner). It consists of two main species of
pl 4.2 and 4.3 has a pH optimum of 4.5 for the hydrolysis of hordein and accounts for over a half of the hordein degrading activity in the malt. It is inhibited by
p-chloromercuriphenolsulphonic acid and leupeptin. MEP-1 also hydrolyses haemoglobin and azocasein and while the activity on the latter is stimulated two-fold by 5 mM 2-mercaptoethanol (2-ME) the hydrolysis of hordein is increased 11-fold at this concentration of the thiol. MEP-1 hydrolysed a range of
N-
t-butoxycarbonyl-
l-amino acid-
p-nitrophenyl esters; the highest activity was obtained with the derivatives of glutamine, alanine and leucine. A polyclonal antibody to MEP-1 cross reacted with a 37 000
M
r
endopeptidase present at low activity. |
| doi_str_mv | 10.1016/0031-9422(89)80332-2 |
| format | article |
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M
r
29 000 which we have named malt endopeptidase-1 (MEP-1) was purified to homogeneity from a four-day green malt of barley (
Hordeum vulgare cv Schooner). It consists of two main species of
pl 4.2 and 4.3 has a pH optimum of 4.5 for the hydrolysis of hordein and accounts for over a half of the hordein degrading activity in the malt. It is inhibited by
p-chloromercuriphenolsulphonic acid and leupeptin. MEP-1 also hydrolyses haemoglobin and azocasein and while the activity on the latter is stimulated two-fold by 5 mM 2-mercaptoethanol (2-ME) the hydrolysis of hordein is increased 11-fold at this concentration of the thiol. MEP-1 hydrolysed a range of
N-
t-butoxycarbonyl-
l-amino acid-
p-nitrophenyl esters; the highest activity was obtained with the derivatives of glutamine, alanine and leucine. A polyclonal antibody to MEP-1 cross reacted with a 37 000
M
r
endopeptidase present at low activity.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><identifier>DOI: 10.1016/0031-9422(89)80332-2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Analytical, structural and metabolic biochemistry ; barley malt ; Biological and medical sciences ; chemical constituents of plants ; chemical degradation ; cysteine ; cysteine endopeptidase ; enzyme activity ; Enzymes and enzyme inhibitors ; food composition ; Fundamental and applied biological sciences. Psychology ; Gramineae ; hordein ; hordein degradation ; Hordeum ; Hordeum vulgare ; Hydrolases ; malt ; proteinases ; purification ; seeds ; substrate specificity</subject><ispartof>Phytochemistry (Oxford), 1989, Vol.28 (12), p.3285-3290</ispartof><rights>1989</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-314c1a53f2ad7f94ac775e8ffbdf9e9b4b9a5b21581bb10e51d1208379f5ead13</citedby><cites>FETCH-LOGICAL-c389t-314c1a53f2ad7f94ac775e8ffbdf9e9b4b9a5b21581bb10e51d1208379f5ead13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0031942289803322$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,786,790,3624,4043,27956,27957,27958,46044</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19311459$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Phillips, Hilary A.</creatorcontrib><creatorcontrib>Wallace, William</creatorcontrib><title>A cysteine endopeptidase from barley malt which degrades hordein</title><title>Phytochemistry (Oxford)</title><description>A cysteine endopeptidase of
M
r
29 000 which we have named malt endopeptidase-1 (MEP-1) was purified to homogeneity from a four-day green malt of barley (
Hordeum vulgare cv Schooner). It consists of two main species of
pl 4.2 and 4.3 has a pH optimum of 4.5 for the hydrolysis of hordein and accounts for over a half of the hordein degrading activity in the malt. It is inhibited by
p-chloromercuriphenolsulphonic acid and leupeptin. MEP-1 also hydrolyses haemoglobin and azocasein and while the activity on the latter is stimulated two-fold by 5 mM 2-mercaptoethanol (2-ME) the hydrolysis of hordein is increased 11-fold at this concentration of the thiol. MEP-1 hydrolysed a range of
N-
t-butoxycarbonyl-
l-amino acid-
p-nitrophenyl esters; the highest activity was obtained with the derivatives of glutamine, alanine and leucine. A polyclonal antibody to MEP-1 cross reacted with a 37 000
M
r
endopeptidase present at low activity.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>barley malt</subject><subject>Biological and medical sciences</subject><subject>chemical constituents of plants</subject><subject>chemical degradation</subject><subject>cysteine</subject><subject>cysteine endopeptidase</subject><subject>enzyme activity</subject><subject>Enzymes and enzyme inhibitors</subject><subject>food composition</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gramineae</subject><subject>hordein</subject><subject>hordein degradation</subject><subject>Hordeum</subject><subject>Hordeum vulgare</subject><subject>Hydrolases</subject><subject>malt</subject><subject>proteinases</subject><subject>purification</subject><subject>seeds</subject><subject>substrate specificity</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNp90MFLHDEUx_EgFrpV_4NC59JiD6N5yWSTXIoitRUWelDP4U3y4qbMzmyTWWX_e2ddsTdPuXx-j_Bl7DPwM-AwP-dcQm0bIU6N_W64lKIWB2wGRstaas4P2eyNfGSfSvnLOVdqPp-xi8vKb8tIqaeK-jCsaT2mgIWqmIdV1WLuaFutsBurp2XyyyrQQ8ZApVoOOUyzY_YhYlfo5PU9YvfXP--ufteLP79uri4XtZfGjrWExgMqGQUGHW2DXmtFJsY2REu2bVqLqhWgDLQtcFIQQHAjtY2KMIA8Yt_2d9d5-LehMrpVKp66DnsaNsWBUloKrSbY7KHPQymZolvntMK8dcDdLpfbtXC7Fs5Y95LLiWn29fU-Fo9dzNj7VP5vrQRolJ3cl72LODh8yJO5vxUcJBdzw7XQk_ixFzTleEyUXfGJek8hZfKjC0N6_yvPvQyHQw</recordid><startdate>1989</startdate><enddate>1989</enddate><creator>Phillips, Hilary A.</creator><creator>Wallace, William</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>1989</creationdate><title>A cysteine endopeptidase from barley malt which degrades hordein</title><author>Phillips, Hilary A. ; Wallace, William</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-314c1a53f2ad7f94ac775e8ffbdf9e9b4b9a5b21581bb10e51d1208379f5ead13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>barley malt</topic><topic>Biological and medical sciences</topic><topic>chemical constituents of plants</topic><topic>chemical degradation</topic><topic>cysteine</topic><topic>cysteine endopeptidase</topic><topic>enzyme activity</topic><topic>Enzymes and enzyme inhibitors</topic><topic>food composition</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gramineae</topic><topic>hordein</topic><topic>hordein degradation</topic><topic>Hordeum</topic><topic>Hordeum vulgare</topic><topic>Hydrolases</topic><topic>malt</topic><topic>proteinases</topic><topic>purification</topic><topic>seeds</topic><topic>substrate specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Phillips, Hilary A.</creatorcontrib><creatorcontrib>Wallace, William</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Phillips, Hilary A.</au><au>Wallace, William</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A cysteine endopeptidase from barley malt which degrades hordein</atitle><jtitle>Phytochemistry (Oxford)</jtitle><date>1989</date><risdate>1989</risdate><volume>28</volume><issue>12</issue><spage>3285</spage><epage>3290</epage><pages>3285-3290</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>A cysteine endopeptidase of
M
r
29 000 which we have named malt endopeptidase-1 (MEP-1) was purified to homogeneity from a four-day green malt of barley (
Hordeum vulgare cv Schooner). It consists of two main species of
pl 4.2 and 4.3 has a pH optimum of 4.5 for the hydrolysis of hordein and accounts for over a half of the hordein degrading activity in the malt. It is inhibited by
p-chloromercuriphenolsulphonic acid and leupeptin. MEP-1 also hydrolyses haemoglobin and azocasein and while the activity on the latter is stimulated two-fold by 5 mM 2-mercaptoethanol (2-ME) the hydrolysis of hordein is increased 11-fold at this concentration of the thiol. MEP-1 hydrolysed a range of
N-
t-butoxycarbonyl-
l-amino acid-
p-nitrophenyl esters; the highest activity was obtained with the derivatives of glutamine, alanine and leucine. A polyclonal antibody to MEP-1 cross reacted with a 37 000
M
r
endopeptidase present at low activity.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><doi>10.1016/0031-9422(89)80332-2</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0031-9422 |
| ispartof | Phytochemistry (Oxford), 1989, Vol.28 (12), p.3285-3290 |
| issn | 0031-9422 1873-3700 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15573275 |
| source | Backfile Package - Organic Chemistry (Legacy) [YCO] |
| subjects | Analytical, structural and metabolic biochemistry barley malt Biological and medical sciences chemical constituents of plants chemical degradation cysteine cysteine endopeptidase enzyme activity Enzymes and enzyme inhibitors food composition Fundamental and applied biological sciences. Psychology Gramineae hordein hordein degradation Hordeum Hordeum vulgare Hydrolases malt proteinases purification seeds substrate specificity |
| title | A cysteine endopeptidase from barley malt which degrades hordein |
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