Isolation and properties of alpha-D-mannosidase from human kidney
Alpha-D-Mannosidase activity exists in three forms that can be separated by DEAE-cellulose chromatography, alpha-D-Mannosidase was isolated from human kidney in a homogeneous state, and was purified 2100-fold, with p-nitrophenyl alpha-D-mannoside as substrate. The purified alpha-D-mannosidase was pr...
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| Veröffentlicht in: | Biochemical journal 1976-05, Vol.155 (2), p.217-223 |
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| creator | Marinkovic, D V Marinkovic, J N |
| description | Alpha-D-Mannosidase activity exists in three forms that can be separated by DEAE-cellulose chromatography, alpha-D-Mannosidase was isolated from human kidney in a homogeneous state, and was purified 2100-fold, with p-nitrophenyl alpha-D-mannoside as substrate. The purified alpha-D-mannosidase was practically free from all other glycosidases tested. The Km of the synthetic substrate with the enzyme was 1 X 10(-3) M and the pH optimum 4.5. It was inhibited by heavy metals, sodium dodecyl sulphate, urea and compounds that react with the thiol groups, and was activated by Zn2+, Na+, 2-mercaptoethanol, human albumin and gamma-globulin. The mol. wt. of the enzyme was estimated to be 180 000 +/- 4500. After pretreatment with 2-mercaptoethanol and sodium dodecyl sulphate, alpha-D-mannosidase dissociated into subunits of mol. wts. of 58 000 +/- 600 and 30 000 +/- 380 respectively. Subunits of the same molecular weights were also obtained after the enzyme was heated at 100 degrees C. |
| doi_str_mv | 10.1042/bj1550217 |
| format | Article |
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The purified alpha-D-mannosidase was practically free from all other glycosidases tested. The Km of the synthetic substrate with the enzyme was 1 X 10(-3) M and the pH optimum 4.5. It was inhibited by heavy metals, sodium dodecyl sulphate, urea and compounds that react with the thiol groups, and was activated by Zn2+, Na+, 2-mercaptoethanol, human albumin and gamma-globulin. The mol. wt. of the enzyme was estimated to be 180 000 +/- 4500. After pretreatment with 2-mercaptoethanol and sodium dodecyl sulphate, alpha-D-mannosidase dissociated into subunits of mol. wts. of 58 000 +/- 600 and 30 000 +/- 380 respectively. Subunits of the same molecular weights were also obtained after the enzyme was heated at 100 degrees C.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj1550217</identifier><identifier>PMID: 7243</identifier><language>eng</language><publisher>England</publisher><subject>Ammonium Sulfate ; Disaccharidases - isolation & purification ; Enzyme Activation ; Hot Temperature ; Humans ; Hydrogen-Ion Concentration ; Kidney - enzymology ; Kinetics ; Mannosidases - analysis ; Mannosidases - antagonists & inhibitors ; Mannosidases - isolation & purification ; Molecular Weight ; Protein Denaturation</subject><ispartof>Biochemical journal, 1976-05, Vol.155 (2), p.217-223</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c367t-85e4ff47c0f944f17df96d7477779eeb28629ed5238891a39c36dd5cd74329453</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1172826/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1172826/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7243$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marinkovic, D V</creatorcontrib><creatorcontrib>Marinkovic, J N</creatorcontrib><title>Isolation and properties of alpha-D-mannosidase from human kidney</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Alpha-D-Mannosidase activity exists in three forms that can be separated by DEAE-cellulose chromatography, alpha-D-Mannosidase was isolated from human kidney in a homogeneous state, and was purified 2100-fold, with p-nitrophenyl alpha-D-mannoside as substrate. The purified alpha-D-mannosidase was practically free from all other glycosidases tested. The Km of the synthetic substrate with the enzyme was 1 X 10(-3) M and the pH optimum 4.5. It was inhibited by heavy metals, sodium dodecyl sulphate, urea and compounds that react with the thiol groups, and was activated by Zn2+, Na+, 2-mercaptoethanol, human albumin and gamma-globulin. The mol. wt. of the enzyme was estimated to be 180 000 +/- 4500. After pretreatment with 2-mercaptoethanol and sodium dodecyl sulphate, alpha-D-mannosidase dissociated into subunits of mol. wts. of 58 000 +/- 600 and 30 000 +/- 380 respectively. Subunits of the same molecular weights were also obtained after the enzyme was heated at 100 degrees C.</description><subject>Ammonium Sulfate</subject><subject>Disaccharidases - isolation & purification</subject><subject>Enzyme Activation</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kidney - enzymology</subject><subject>Kinetics</subject><subject>Mannosidases - analysis</subject><subject>Mannosidases - antagonists & inhibitors</subject><subject>Mannosidases - isolation & purification</subject><subject>Molecular Weight</subject><subject>Protein Denaturation</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkM1LAzEQxYNUtFYPXj3tSfCwmq_d7F6EUr8KBS96DulmYlN3kzXZCv3vTbEUncvAvN-8GR5ClwTfEszp3XJNigJTIo7QmHCB80rQaoTGmJY8L5Nwis5iXGNMOOb4BI0E5WyMpvPoWzVY7zLldNYH30MYLMTMm0y1_UrlD3mnnPPRahUhM8F32WqTRtmn1Q625-jYqDbCxb5P0PvT49vsJV-8Ps9n00XesFIMeVUAN4aLBpuac0OENnWpBRepaoAlrUpagy4oq6qaKFanNa2LJiGM1rxgE3T_69tvlh3oBtwQVCv7YDsVttIrK_8rzq7kh_-WhKQkaJkMrvcGwX9tIA6ys7GBtlUO_CbKivFUlCXw5hdsgo8xgDkcIVjuwpaHsBN79ferA7lLl_0AG4N5zg</recordid><startdate>19760501</startdate><enddate>19760501</enddate><creator>Marinkovic, D V</creator><creator>Marinkovic, J N</creator><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><scope>5PM</scope></search><sort><creationdate>19760501</creationdate><title>Isolation and properties of alpha-D-mannosidase from human kidney</title><author>Marinkovic, D V ; Marinkovic, J N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c367t-85e4ff47c0f944f17df96d7477779eeb28629ed5238891a39c36dd5cd74329453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Ammonium Sulfate</topic><topic>Disaccharidases - isolation & purification</topic><topic>Enzyme Activation</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kidney - enzymology</topic><topic>Kinetics</topic><topic>Mannosidases - analysis</topic><topic>Mannosidases - antagonists & inhibitors</topic><topic>Mannosidases - isolation & purification</topic><topic>Molecular Weight</topic><topic>Protein Denaturation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marinkovic, D V</creatorcontrib><creatorcontrib>Marinkovic, J N</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marinkovic, D V</au><au>Marinkovic, J N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and properties of alpha-D-mannosidase from human kidney</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1976-05-01</date><risdate>1976</risdate><volume>155</volume><issue>2</issue><spage>217</spage><epage>223</epage><pages>217-223</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Alpha-D-Mannosidase activity exists in three forms that can be separated by DEAE-cellulose chromatography, alpha-D-Mannosidase was isolated from human kidney in a homogeneous state, and was purified 2100-fold, with p-nitrophenyl alpha-D-mannoside as substrate. The purified alpha-D-mannosidase was practically free from all other glycosidases tested. The Km of the synthetic substrate with the enzyme was 1 X 10(-3) M and the pH optimum 4.5. It was inhibited by heavy metals, sodium dodecyl sulphate, urea and compounds that react with the thiol groups, and was activated by Zn2+, Na+, 2-mercaptoethanol, human albumin and gamma-globulin. The mol. wt. of the enzyme was estimated to be 180 000 +/- 4500. After pretreatment with 2-mercaptoethanol and sodium dodecyl sulphate, alpha-D-mannosidase dissociated into subunits of mol. wts. of 58 000 +/- 600 and 30 000 +/- 380 respectively. Subunits of the same molecular weights were also obtained after the enzyme was heated at 100 degrees C.</abstract><cop>England</cop><pmid>7243</pmid><doi>10.1042/bj1550217</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1976-05, Vol.155 (2), p.217-223 |
| issn | 0264-6021 1470-8728 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1172826 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Ammonium Sulfate Disaccharidases - isolation & purification Enzyme Activation Hot Temperature Humans Hydrogen-Ion Concentration Kidney - enzymology Kinetics Mannosidases - analysis Mannosidases - antagonists & inhibitors Mannosidases - isolation & purification Molecular Weight Protein Denaturation |
| title | Isolation and properties of alpha-D-mannosidase from human kidney |
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