Linked Life Data

6114095

Source:http://linkedlifedata.com/resource/pubmed/id/6114095

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1981-9-15
pubmed:abstractText
Nucleotide pyrophosphatase, a Zn2+-dependent enzyme catalyzing the hydrolysis of sugar nucleotides, generally interferes with glycosyltransferase assays. Certain tissues such as intestinal mucosa are particularly rich sources of nucleotide pyrophosphatase activity. The inhibition of nucleotide pyrophosphatase without affecting glycosyltransferase activities by the removal of Zn2+ allows for the assay of galactosyltransferases in rat intestinal particulate fractions. Inactivation of nucleotide pyrophosphatase was achieved by preincubation of particulate enzyme preparations in the presence of EDTA. Addition of Mn2+, required for the galactosyltransferase assays, did not reactivate the nucleotide pyrophosphatase. The presence of 0.05% (w/v) soybean trypsin inhibitor was required during the preparation of intestinal mucosa homogenates and enzyme assays to protect the UDP-galactose: N-acetylglucosaminyl galactosyltransferase from inactivation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7142-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Galactosyltransferase activities in rat intestinal mucosa. Inhibition of nucleotide pyrophosphatase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.