Linked Life Data

3982559

Source:http://linkedlifedata.com/resource/pubmed/id/3982559

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-5-1
pubmed:abstractText
Thermostability of the purified alkaline phosphatase derived from human uterine muscle and myoma was established before and after desialization. Both enzymes were inhibited by sucrose, glucose and maltose in proportion to the carbohydrate concentration. L-Homoarginine inhibits the myoma enzyme in 90%, L-leucine, L-histidine and L-tryptophan in about 60%, and L-phenylalanine in less than 15%. The type of inhibition and Ki values were determined. Muscle and myoma enzymes cross-reacted with antisera against human liver and placental isoenzymes. Molecular and kinetic properties of the enzyme were compared with known human isoenzymes of alkaline phosphatase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-2685
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-43
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Alkaline phosphatase from human uterine myoma. II. Kinetic and immunological properties.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't