| Aggregation-dissociation and stability of acid beta-galactosidase purified from porcine spleen. | |
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MedLine Citation:
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PMID: 3086147 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sucrose gradient centrifugation of the monomeric form (A1) of porcine spleen beta-galactosidase showed a pH-dependent equilibrium between monomer at neutral pH (pH 7.0) and dimer at acidic pH (pH 5.4-3.0), independent of ionic strength. While the oligomeric form (Ao), which was hardly dissociated under physiological conditions, was dissociated only with some protein denaturing agents into similar catalytic subunit to the A1. Both the A1 and Ao were equally active and stable at acidic pH, in the physiological condition inside lysosome (around pH 4.6). |
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Authors:
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Y Yamamoto; K Nishimura |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: The International journal of biochemistry Volume: 18 ISSN: 0020-711X ISO Abbreviation: Int. J. Biochem. Publication Date: 1986 |
Date Detail:
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Created Date: 1986-07-15 Completed Date: 1986-07-15 Revised Date: 2004-11-17 |
Medline Journal Info:
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Nlm Unique ID: 0250365 Medline TA: Int J Biochem Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 327-35 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Centrifugation, Density Gradient Drug Stability Galactosidases / metabolism* Hydrogen-Ion Concentration Kinetics Macromolecular Substances Molecular Weight Spleen / enzymology* Swine Thermodynamics beta-Galactosidase / isolation & purification, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Macromolecular Substances; EC 3.2.1.-/Galactosidases; EC 3.2.1.23/beta-Galactosidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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