Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-1-14
pubmed:abstractText
An acid alpha-glucosidase (EC 3.2.1.3) has been purified to electrophoretic homogeneity from the soluble fraction of the human term placenta. In the presence of SDS, two doublets of 79 and 67 kDa were seen in addition to other bands of extremely low intensity. Each of these bands was seen to cross-react with polyclonal antiserum raised to the purified enzyme, thus confirming the homogeneity of the preparation. The purified enzyme exhibited a broad substrate specificity. The kinetic data revealed the possible presence of multiple substrate binding sites. Chemical modification using group specific reagents indicated the presence of a carboxyl group and tryptophan at the active site. Based on these results a possible structure for the active site of the human term placental acid alpha-glucosidase has been proposed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1051-61
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Purification and biochemical characterisation of human placental acid alpha-glucosidase.
pubmed:affiliation
Department of Life Sciences, University of Bombay, India.
pubmed:publicationType
Journal Article