| pubmed-article:2139328 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C0005270 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C1512310 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C0765250 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:2139328 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:2139328 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2139328 | pubmed:dateCreated | 1990-5-16 | lld:pubmed |
| pubmed-article:2139328 | pubmed:abstractText | Extracts of the human promyelocytic cell line HL-60 contain a form of beta-N-acetylhexosaminidase that is not retained on columns of benzeneboronate-agarose ('phenylboronate-agarose') and has a pI value lower than that of beta-N-acetylhexosaminidase A. It is clearly distinct from beta-N-acetylhexosaminidase A in its behaviour on DEAE-cellulose columns, and it requires a higher concentration of salt for its elution. This 'extra' form has a higher ratio of activity towards 4-methylumbelliferyl beta-N-acetylglucosaminide 6-sulphate and 4-methylumbelliferyl beta-N-acetylglucosaminide than has beta-N-acetylhexosaminidase A and is less stable when heated at 50 degrees C. It has a pH optimum of 4.5 and is therefore not beta-N-acetylglucosaminidase C. Anti-(human beta-N-acetylhexosaminidase alpha-subunit) serum precipitated both beta-N-acetylhexosaminidase A and the 'extra' form, whereas an anti-(beta-subunit) serum precipitated beta-N-acetylhexosaminidase A but not the 'extra' form. Western blotting and immunodetection of polypeptides derived from the 'extra' form revealed a band corresponding in size to mature alpha-subunits. On the basis of this and of its behaviour on isoelectric focusing, chromatofocusing and its kinetic properties, we conclude that the 'extra' form is composed of alpha-subunits and resembles beta-N-acetylhexosaminidase S, the residual form in Sandhoff's disease. | lld:pubmed |
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| pubmed-article:2139328 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2139328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2139328 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2139328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2139328 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2139328 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2139328 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2139328 | pubmed:author | pubmed-author:StirlingJ LJL | lld:pubmed |
| pubmed-article:2139328 | pubmed:author | pubmed-author:OrlacchioAA | lld:pubmed |
| pubmed-article:2139328 | pubmed:author | pubmed-author:EmilianiCC | lld:pubmed |
| pubmed-article:2139328 | pubmed:author | pubmed-author:BeccariTT | lld:pubmed |
| pubmed-article:2139328 | pubmed:author | pubmed-author:TabilioAA | lld:pubmed |
| pubmed-article:2139328 | pubmed:author | pubmed-author:HosseiniRR | lld:pubmed |
| pubmed-article:2139328 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2139328 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2139328 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:2139328 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2139328 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2139328 | pubmed:pagination | 111-7 | lld:pubmed |
| pubmed-article:2139328 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2139328 | pubmed:meshHeading | pubmed-meshheading:2139328-... | lld:pubmed |
| pubmed-article:2139328 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2139328 | pubmed:articleTitle | An enzyme with properties similar to those of beta-N-acetylhexosaminidase S is expressed in the promyelocytic cell line HL-60. | lld:pubmed |
| pubmed-article:2139328 | pubmed:affiliation | Dipartimento di Medicina Sperimentale e Scienze Biochemiche, Università di Perugia, Italy. | lld:pubmed |
| pubmed-article:2139328 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2139328 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2139328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2139328 | lld:pubmed |
