Linked Life Data

1415104

Source:http://linkedlifedata.com/resource/pubmed/id/1415104

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1992-11-6
pubmed:abstractText
Sulfation plays a major role in the processing of secretory proteins. We report here on tyrosylprotein sulfotransferase activity in human gastric mucosa of normal and alcoholics. The tyrosylprotein sulfotransferase was identified in the Golgi-enriched fraction. In alcoholics, the activity of sulfotransferase was 2- to 3-fold higher than in normals. However, no change in the activity of UDP-glucose-ceramide glucosyltransferase, a marker for Golgi, between alcoholics and normals was observed. The tyrosylprotein sulfotransferase enzyme required Triton X-100, MnCl2 and 5'-AMP, and obtained optimum activity at pH 6.8 in the presence of 0.5% Triton X-100, 20 mM MnCl2, 50 mM NaF, and 2 mM 5'-AMP. The apparent Km for poly-Glu6, Ala3, Tyr1 (EAY; 47,000) was 1.9 x 10(-6) M and for 3'-phosphoadenosine 5'-phosphosulfate (PAPS), 1.4 x 10(-6) M. The results suggest that alcohol abuse causes enhancement in the expression of gastric mucosal tyrosylprotein sulfotransferase activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0002-9270
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1460-3
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Tyrosylprotein sulfotransferase activity is increased in human gastric mucosa of alcoholics.
pubmed:affiliation
New Jersey Dental School, Department of Medicine, University of Medicine and Dentistry of New Jersey, Newark.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't