Identification of beta-N-acetylhexosaminidase A in mouse tissues with the fluorigenic substrate 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate
beta-N-Acetylhexosaminidase from mouse tissue was separated into its constituent isoenzymes on DEAE-cellulose and its activity was monitored with 4-methylumbelliferyl-beta-N-acetylglucosamine and 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate. Forms corresponding to the human isoenzymes A...
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| Veröffentlicht in: | Biochemical journal 1988-06, Vol.252 (2), p.617-620 |
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| container_title | Biochemical journal |
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| creator | Beccari, T Orlacchio, A Stirling, J L |
| description | beta-N-Acetylhexosaminidase from mouse tissue was separated into its constituent isoenzymes on DEAE-cellulose and its activity was monitored with 4-methylumbelliferyl-beta-N-acetylglucosamine and 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate. Forms corresponding to the human isoenzymes A (acidic), B (basic) and an 'intermediate' form were present in mouse liver and spleen, whereas in kidney the B and 'intermediate' forms predominated, with A present only as a minor component. In brain the 'intermediate', A and C activities were detected. Testis had predominantly A activity, whereas epididymis, the tissue with the highest specific activity of beta-N-acetylhexosaminidase, had an abundance of the 'intermediate' form, but was almost entirely lacking in the A form. |
| doi_str_mv | 10.1042/bj2520617 |
| format | Article |
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Forms corresponding to the human isoenzymes A (acidic), B (basic) and an 'intermediate' form were present in mouse liver and spleen, whereas in kidney the B and 'intermediate' forms predominated, with A present only as a minor component. In brain the 'intermediate', A and C activities were detected. 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Forms corresponding to the human isoenzymes A (acidic), B (basic) and an 'intermediate' form were present in mouse liver and spleen, whereas in kidney the B and 'intermediate' forms predominated, with A present only as a minor component. In brain the 'intermediate', A and C activities were detected. Testis had predominantly A activity, whereas epididymis, the tissue with the highest specific activity of beta-N-acetylhexosaminidase, had an abundance of the 'intermediate' form, but was almost entirely lacking in the A form.</description><subject>Animals</subject><subject>beta-N-Acetylhexosaminidases - isolation & purification</subject><subject>beta-N-Acetylhexosaminidases - metabolism</subject><subject>Brain - enzymology</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Hymecromone - analogs & derivatives</subject><subject>Kidney - enzymology</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Spleen - enzymology</subject><subject>Testis - enzymology</subject><subject>Tissue Distribution</subject><subject>Umbelliferones</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhS0EKkNhwQMgeYXEwtR2nNjZIFUVP5WqsmnXln-uJ66cZIidwrwJj4vRjEZ0xcpX8nfPvfcchN4y-pFRwS_sA2857Zh8hjZMSEqU5Oo52lDeCdJRzl6iVzk_UMoEFfQMnfFeUiW6Dfp97WEqMURnSpwnPAdsoRhyS4yDsk8D_JqzGeMUvcmAL3Gc8DivtSwx5xUy_hnLgMsAOKR1XuIWpuhwXm0uiymABRmhDPu0jhZSigGWfSJPRmzT6g4zAHckr2k31MbX6EUwKcOb43uO7r98vrv6Rm6-f72-urwhTlBWSBMsb9rgbde3fd8Jy0zvIHhvJFOt90yyxnKnpGyAei7aRvVc9D24IDojbHOOPh10d6sdwbvqxmKS3i1xNMtezybqpz9THPR2ftSMiZ4pWQXeHwWW-Uc1pOgxZldvNRNUo7RUgireNv8FWcskFR2r4IcD6JY55wXCaRtG9d-89Snvyr77d_0TeQy4-QNrJ6qU</recordid><startdate>19880601</startdate><enddate>19880601</enddate><creator>Beccari, T</creator><creator>Orlacchio, A</creator><creator>Stirling, J L</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19880601</creationdate><title>Identification of beta-N-acetylhexosaminidase A in mouse tissues with the fluorigenic substrate 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate</title><author>Beccari, T ; Orlacchio, A ; Stirling, J L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-3fb235fdb6959964b1a9cefdda7185dd1713b2c8773e0d2453892499ecf46a4b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>beta-N-Acetylhexosaminidases - isolation & purification</topic><topic>beta-N-Acetylhexosaminidases - metabolism</topic><topic>Brain - enzymology</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Hymecromone - analogs & derivatives</topic><topic>Kidney - enzymology</topic><topic>Liver - enzymology</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Spleen - enzymology</topic><topic>Testis - enzymology</topic><topic>Tissue Distribution</topic><topic>Umbelliferones</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Beccari, T</creatorcontrib><creatorcontrib>Orlacchio, A</creatorcontrib><creatorcontrib>Stirling, J 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>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><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>Beccari, T</au><au>Orlacchio, A</au><au>Stirling, J L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of beta-N-acetylhexosaminidase A in mouse tissues with the fluorigenic substrate 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1988-06-01</date><risdate>1988</risdate><volume>252</volume><issue>2</issue><spage>617</spage><epage>620</epage><pages>617-620</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>beta-N-Acetylhexosaminidase from mouse tissue was separated into its constituent isoenzymes on DEAE-cellulose and its activity was monitored with 4-methylumbelliferyl-beta-N-acetylglucosamine and 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate. Forms corresponding to the human isoenzymes A (acidic), B (basic) and an 'intermediate' form were present in mouse liver and spleen, whereas in kidney the B and 'intermediate' forms predominated, with A present only as a minor component. In brain the 'intermediate', A and C activities were detected. Testis had predominantly A activity, whereas epididymis, the tissue with the highest specific activity of beta-N-acetylhexosaminidase, had an abundance of the 'intermediate' form, but was almost entirely lacking in the A form.</abstract><cop>England</cop><pmid>2970846</pmid><doi>10.1042/bj2520617</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1988-06, Vol.252 (2), p.617-620 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals beta-N-Acetylhexosaminidases - isolation & purification beta-N-Acetylhexosaminidases - metabolism Brain - enzymology Chromatography, DEAE-Cellulose Hymecromone - analogs & derivatives Kidney - enzymology Liver - enzymology Male Mice Mice, Inbred BALB C Spleen - enzymology Testis - enzymology Tissue Distribution Umbelliferones |
| title | Identification of beta-N-acetylhexosaminidase A in mouse tissues with the fluorigenic substrate 4-methylumbelliferyl-beta-N-acetylglucosamine 6-sulphate |
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