Bacillus subtilis aminopeptidase: Purification, characterization and some enzymatic properties
The extracellular aminopeptidase from Bacillus subtilis was purified 300-fold by a simple procedure which gave a high recovery of enzyme. The native enzyme was shown to be a monomer of molecular weight 46,500 and to contain 1 g-atom of Zn 2+ per mole of protein. Amino acid analyses demonstrated the...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1979-10, Vol.197 (1), p.63-72 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 197 |
| creator | Wagner, Fred W. Ray, Lee E. Ajabnoor, Mohammed A. Ziemba, Paul E. Hall, R.L. |
| description | The extracellular aminopeptidase from
Bacillus subtilis was purified 300-fold by a simple procedure which gave a high recovery of enzyme. The native enzyme was shown to be a monomer of molecular weight 46,500 and to contain 1 g-atom of Zn
2+ per mole of protein. Amino acid analyses demonstrated the protein to be rich in acidic residues and Lys, to possess about 3 residues of Met, and to be devoid of Cys. When activated with 5 m
m Co(NO
3)
2 for 90 min the activity of the native enzyme was increased; the amount of activation depended on the identity of the substrate. Cobalt activation involved the reversible binding of 1 g-atom of Co
2+ per mole of protein, without displacing the native Zn
2+;
K
Co was 1.25 m
m. Zinc ions competed with Co
2+ during activation, a process characterized by a
K
Zn
of 28 μ
m. Ions other than Co
2+ did not appreciably activate the enzyme. |
| doi_str_mv | 10.1016/0003-9861(79)90219-4 |
| format | Article |
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Bacillus subtilis was purified 300-fold by a simple procedure which gave a high recovery of enzyme. The native enzyme was shown to be a monomer of molecular weight 46,500 and to contain 1 g-atom of Zn
2+ per mole of protein. Amino acid analyses demonstrated the protein to be rich in acidic residues and Lys, to possess about 3 residues of Met, and to be devoid of Cys. When activated with 5 m
m Co(NO
3)
2 for 90 min the activity of the native enzyme was increased; the amount of activation depended on the identity of the substrate. Cobalt activation involved the reversible binding of 1 g-atom of Co
2+ per mole of protein, without displacing the native Zn
2+;
K
Co was 1.25 m
m. Zinc ions competed with Co
2+ during activation, a process characterized by a
K
Zn
of 28 μ
m. Ions other than Co
2+ did not appreciably activate the enzyme.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(79)90219-4</identifier><identifier>PMID: 120703</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acids - analysis ; Aminopeptidases - isolation & purification ; Aminopeptidases - metabolism ; Bacillus subtilis - enzymology ; Binding Sites ; Chemical Phenomena ; Chemistry ; Enzyme Activation - drug effects ; Molecular Weight ; Zinc - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 1979-10, Vol.197 (1), p.63-72</ispartof><rights>1979</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-377402e79edffa85543eeec3461bee04e30e4c85a7945abb3b5113732ea101773</citedby><cites>FETCH-LOGICAL-c422t-377402e79edffa85543eeec3461bee04e30e4c85a7945abb3b5113732ea101773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986179902194$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/120703$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wagner, Fred W.</creatorcontrib><creatorcontrib>Ray, Lee E.</creatorcontrib><creatorcontrib>Ajabnoor, Mohammed A.</creatorcontrib><creatorcontrib>Ziemba, Paul E.</creatorcontrib><creatorcontrib>Hall, R.L.</creatorcontrib><title>Bacillus subtilis aminopeptidase: Purification, characterization and some enzymatic properties</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The extracellular aminopeptidase from
Bacillus subtilis was purified 300-fold by a simple procedure which gave a high recovery of enzyme. The native enzyme was shown to be a monomer of molecular weight 46,500 and to contain 1 g-atom of Zn
2+ per mole of protein. Amino acid analyses demonstrated the protein to be rich in acidic residues and Lys, to possess about 3 residues of Met, and to be devoid of Cys. When activated with 5 m
m Co(NO
3)
2 for 90 min the activity of the native enzyme was increased; the amount of activation depended on the identity of the substrate. Cobalt activation involved the reversible binding of 1 g-atom of Co
2+ per mole of protein, without displacing the native Zn
2+;
K
Co was 1.25 m
m. Zinc ions competed with Co
2+ during activation, a process characterized by a
K
Zn
of 28 μ
m. Ions other than Co
2+ did not appreciably activate the enzyme.</description><subject>Amino Acids - analysis</subject><subject>Aminopeptidases - isolation & purification</subject><subject>Aminopeptidases - metabolism</subject><subject>Bacillus subtilis - enzymology</subject><subject>Binding Sites</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Enzyme Activation - drug effects</subject><subject>Molecular Weight</subject><subject>Zinc - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAUhYP4Gkf_gYusRMFq0qRN40LQwRcM6EK3hjS9xUgfY5IKM7_ezAPdubpw7jnncj-Ejim5oITml4QQlsgip6dCnkmSUpnwLTSiROYJYQXfRqNfyz468P6TEEp5nu6hXZoSQdgIvd9qY5tm8NgPZbCN9Vi3tutnMAu20h6u8MvgbG2NDrbvzrH50E6bAM4uVgrWXYV93wKGbjFvo2bwzMW8Cxb8IdqpdePhaDPH6O3-7nXymEyfH54mN9PE8DQNCROCkxSEhKqudZFlnAGAYTynJQDhwAhwU2RaSJ7psmRlRikTLAUdSQjBxuhk3RtPfw3gg2qtN9A0uoN-8EpwKQVlNBr52mhc772DWs2cbbWbK0rUkqpaIlNLZEpItaKqeIwdb_qHsoXqL7TCGNfX6zXEH78tOOWNhc5AZR2YoKre_t__A1jwh98</recordid><startdate>19791001</startdate><enddate>19791001</enddate><creator>Wagner, Fred W.</creator><creator>Ray, Lee E.</creator><creator>Ajabnoor, Mohammed A.</creator><creator>Ziemba, Paul E.</creator><creator>Hall, R.L.</creator><general>Elsevier Inc</general><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>19791001</creationdate><title>Bacillus subtilis aminopeptidase: Purification, characterization and some enzymatic properties</title><author>Wagner, Fred W. ; Ray, Lee E. ; Ajabnoor, Mohammed A. ; Ziemba, Paul E. ; Hall, R.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-377402e79edffa85543eeec3461bee04e30e4c85a7945abb3b5113732ea101773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Amino Acids - analysis</topic><topic>Aminopeptidases - isolation & purification</topic><topic>Aminopeptidases - metabolism</topic><topic>Bacillus subtilis - enzymology</topic><topic>Binding Sites</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Enzyme Activation - drug effects</topic><topic>Molecular Weight</topic><topic>Zinc - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wagner, Fred W.</creatorcontrib><creatorcontrib>Ray, Lee E.</creatorcontrib><creatorcontrib>Ajabnoor, Mohammed A.</creatorcontrib><creatorcontrib>Ziemba, Paul E.</creatorcontrib><creatorcontrib>Hall, R.L.</creatorcontrib><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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wagner, Fred W.</au><au>Ray, Lee E.</au><au>Ajabnoor, Mohammed A.</au><au>Ziemba, Paul E.</au><au>Hall, R.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bacillus subtilis aminopeptidase: Purification, characterization and some enzymatic properties</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1979-10-01</date><risdate>1979</risdate><volume>197</volume><issue>1</issue><spage>63</spage><epage>72</epage><pages>63-72</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The extracellular aminopeptidase from
Bacillus subtilis was purified 300-fold by a simple procedure which gave a high recovery of enzyme. The native enzyme was shown to be a monomer of molecular weight 46,500 and to contain 1 g-atom of Zn
2+ per mole of protein. Amino acid analyses demonstrated the protein to be rich in acidic residues and Lys, to possess about 3 residues of Met, and to be devoid of Cys. When activated with 5 m
m Co(NO
3)
2 for 90 min the activity of the native enzyme was increased; the amount of activation depended on the identity of the substrate. Cobalt activation involved the reversible binding of 1 g-atom of Co
2+ per mole of protein, without displacing the native Zn
2+;
K
Co was 1.25 m
m. Zinc ions competed with Co
2+ during activation, a process characterized by a
K
Zn
of 28 μ
m. Ions other than Co
2+ did not appreciably activate the enzyme.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>120703</pmid><doi>10.1016/0003-9861(79)90219-4</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1979-10, Vol.197 (1), p.63-72 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74997131 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acids - analysis Aminopeptidases - isolation & purification Aminopeptidases - metabolism Bacillus subtilis - enzymology Binding Sites Chemical Phenomena Chemistry Enzyme Activation - drug effects Molecular Weight Zinc - metabolism |
| title | Bacillus subtilis aminopeptidase: Purification, characterization and some enzymatic properties |
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