Source:http://linkedlifedata.com/resource/pubmed/id/11257525
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-3-21
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pubmed:abstractText |
High molecular weight zinc ion-dependent acid p-nitrophenylphosphatase (HMW-ZnAPase) was purified from bovine liver to homogeneity as judged by native and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The partial sequence of the purified enzyme electroblotted on PVDF membrane reveals a 95% sequence homology with human and bovine liver fructose-1,6-bisphosphate aldolase isozyme B (FALD B). FALD B was isolated from bovine liver using an affinity elution from phosphocellulose column. FALD B from bovine liver shows a native and subunit molecular weight that is indistinguishable from that of HMW-ZnAPase. In addition, an affinity purified antiserum raised in rabbits against purified HMW-ZnAPase cross-reacts with bovine liver FALD B and rabbit muscle isozymes. Despite these similarities, HMW-ZnAPase does not show FALD activity and bovine liver FALD does not display any zinc ion-p-nitrophenylphosphatase activity. These results suggested the existence of structural and immunological similarities between bovine liver HMW-ZnAPase and FALD B. Differences in some amino acid residues in enzyme activity indicate that they may be involved in different biochemical functions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-Nitrophenylphosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose-Bisphosphate Aldolase,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Zinc
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
1546
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
226-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11257525-4-Nitrophenylphosphatase,
pubmed-meshheading:11257525-Amino Acid Sequence,
pubmed-meshheading:11257525-Animals,
pubmed-meshheading:11257525-Blotting, Western,
pubmed-meshheading:11257525-Cattle,
pubmed-meshheading:11257525-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11257525-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:11257525-Humans,
pubmed-meshheading:11257525-Ions,
pubmed-meshheading:11257525-Isoenzymes,
pubmed-meshheading:11257525-Liver,
pubmed-meshheading:11257525-Molecular Sequence Data,
pubmed-meshheading:11257525-Molecular Weight,
pubmed-meshheading:11257525-Zinc
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pubmed:year |
2001
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pubmed:articleTitle |
Structural and immunological similarities between high molecular weight zinc ion-dependent p-nitrophenylphosphatase and fructose-1,6-bisphosphate aldolase from bovine liver.
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pubmed:affiliation |
Department of Cell and Molecular Biology, University of Perugia I-06123, Via Pascoli, I-06123 Perugia, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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