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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1990-5-16
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-14344254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-200169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-2423070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-271272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-2948528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-2965573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-3017984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-304526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-3158659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-3487378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-3488138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-5069351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-5650361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-6234884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-6236812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-6262581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-6324783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-6328091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-7378875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2139328-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
111-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2139328-Blotting, Western,
pubmed-meshheading:2139328-Chromatography,
pubmed-meshheading:2139328-Chromatography, DEAE-Cellulose,
pubmed-meshheading:2139328-Chromatography, Gel,
pubmed-meshheading:2139328-Drug Stability,
pubmed-meshheading:2139328-Granulocytes,
pubmed-meshheading:2139328-Hot Temperature,
pubmed-meshheading:2139328-Humans,
pubmed-meshheading:2139328-Isoelectric Focusing,
pubmed-meshheading:2139328-Kinetics,
pubmed-meshheading:2139328-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:2139328-Sepharose,
pubmed-meshheading:2139328-Substrate Specificity,
pubmed-meshheading:2139328-Tumor Cells, Cultured,
pubmed-meshheading:2139328-beta-N-Acetylhexosaminidases
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pubmed:year |
1990
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pubmed:articleTitle |
An enzyme with properties similar to those of beta-N-acetylhexosaminidase S is expressed in the promyelocytic cell line HL-60.
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pubmed:affiliation |
Dipartimento di Medicina Sperimentale e Scienze Biochemiche, Università di Perugia, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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