| pubmed-article:8828798 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0037733 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C1262902 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0427623 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0873011 | lld:lifeskim |
| pubmed-article:8828798 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:8828798 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8828798 | pubmed:dateCreated | 1996-12-3 | lld:pubmed |
| pubmed-article:8828798 | pubmed:abstractText | A cDNA encoding soybean alpha-D-galactosidase [E.C. 3.2.1.22] was obtained by screening a soybean library with Phaseolus alpha-D-galactosidase cDNA. The Glycine max alpha-D-galactosidase cDNA is 1.75 kb long and contains untranslated 5' and 3' sequences. The deduced amino acid sequence of the soybean gene has a high degree of homology with other eucaryotic alpha-D-galactosidases. Recombinant alpha-D-galactosidase (rGal) was expressed in Pichia pastoris and purified by affinity chromatography. Purified rGal was homogeneous as judged by SDS-PAGE analysis with the relative molecular mass under reducing conditions of 39.8, and under nonreducing conditions 38.0 kDa. The expressed protein contained the sequence NGLGHTPPMG at the N-terminus, corresponding to the deduced amino acid sequence of the soybean gene. The relative native molecular mass by Sephacryl S-200 chromatography was determined to be 33.1 kDa. The specific activity was 295.6 mumoles of PNP-alpha-D-galactopyranoside hydrolyzed per mg pure rGal per min. rGal was highly specific for alpha-D-galactosyl residues. No detectable hemagglutinin or protease activity was present in the preparations. Furthermore, rGal was active against the blood group B antigen in native human erythrocyte cell suspension assays. The only detectable erythrocyte phenotypic change was loss of the B and P1 epitopes. Consequently, recombinant Glycine max alpha-D-galactosidase may have useful biotechnical applications in the potential mass production of universally transfusable type O erythrocytes by enzymatic conversion. | lld:pubmed |
| pubmed-article:8828798 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8828798 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8828798 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8828798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8828798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8828798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8828798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8828798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8828798 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8828798 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8828798 | pubmed:issn | 1039-9712 | lld:pubmed |
| pubmed-article:8828798 | pubmed:author | pubmed-author:JohnsonS ASA | lld:pubmed |
| pubmed-article:8828798 | pubmed:author | pubmed-author:SmithD SDS | lld:pubmed |
| pubmed-article:8828798 | pubmed:author | pubmed-author:WalkerJ CJC | lld:pubmed |
| pubmed-article:8828798 | pubmed:author | pubmed-author:DavisM OMO | lld:pubmed |
| pubmed-article:8828798 | pubmed:author | pubmed-author:HataD JDJ | lld:pubmed |
| pubmed-article:8828798 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8828798 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:8828798 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8828798 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8828798 | pubmed:pagination | 471-85 | lld:pubmed |
| pubmed-article:8828798 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:8828798 | pubmed:meshHeading | pubmed-meshheading:8828798-... | lld:pubmed |
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| pubmed-article:8828798 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8828798 | pubmed:articleTitle | Cloning, expression and characterization of a blood group B active recombinant alpha-D-galactosidase from soybean (Glycine max). | lld:pubmed |
| pubmed-article:8828798 | pubmed:affiliation | Division of Biological Sciences, University of Missouri, Columbia 65212, USA. | lld:pubmed |
| pubmed-article:8828798 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8828798 | lld:pubmed |
