Linked Life Data

6952825

Source:http://linkedlifedata.com/resource/pubmed/id/6952825

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-7-8
pubmed:abstractText
At least two types of acid phosphatases with markedly different properties were separated from the enamel organ of rat molar tooth buds. One enzyme (A) bound weakly to the CM-cellulose column and was eluted with a combined linear salt and pH gradient; another enzyme (B) bound strongly to the column and was eluted with a second linear salt gradient at constant pH. Enzyme A was identified as a phosphomonoester hydrolase (3.1.3.2) similar to the lysosomal enzyme of soft tissues and the tartrate-sensitive enzyme of bone. Enzyme B did not hydrolyse aliphatic monophosphate ester substrates but, like enzyme A, it did split the aryl monophosphate ester substrate, para-nitrophenylphosphate, as well as the phosphate esters of casein and the acid anhydride substrates, ATP and inorganic pyrophosphate. This enzyme is similar to the low molecular weight tartrate-resistant acid phosphatases of bone and soft tissues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0003-9969
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-32
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Separation and partial purification of acid phosphates of the enamel organ of rat molars.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.