Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1976-3-1
pubmed:abstractText
The enzyme inorganic pyrophosphatase (PPiase, EC 3.6.1.1) from the odontoblastic layer of rat incisors has been studied by means of a radiochemical micromethod. The enzyme was incubated with 32P-pyrophosphate in tris-HCl buffer at 37 degrees C. The reaction was linear with time for at least 45 min, and the pH optimum was found to be 8.8, independent of the amount of pyrophosphate present. Heating the enzyme at 56 degrees C inhibited the enzyme activity rapidly, Mg2+ ions activated the enzyme by 15% at an ion concentration of 4 mM, while higher concentrations were inhibitory. Ca2+ ions and PO43-ions inhibited the enzyme at all concentrations. F- ions did not affect the PPiase at concentrations below 8 mM, whereas higher concentrations had an inhibiting effect. Urea was found to inhibit the enzyme at concentrations above 1.5 M, while EDTA was a strong inhibitor at very low concentrations. The characteristics of PPiase agree well with the properties of the enzyme nonspecific alkaline phosphatase (EC 3.1.3.1.) studied earlier.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0029-845X
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
365-9
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Determination of inorganic pyrophosphatase in rat odontoblast layer by a radiochemical method.
pubmed:publicationType
Journal Article