Linked Life Data

1541002

Source:http://linkedlifedata.com/resource/pubmed/id/1541002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-4-3
pubmed:abstractText
We describe a kinetic colorimetric method for assaying lipase (EC 3.1.1.3) activity in serum by using a natural long-chain fatty acid 1,2-diglyceride. In the presence of colipase, deoxycholate, and calcium ions, pancreatic lipase hydrolyzes the clear substrate solution to produce a 2-monoglyceride, which in turn releases glycerol by the action of a 2-monoglyceride lipase. Glycerol is then assayed by a sequence of enzymatic actions (glycerol kinase, glycerol phosphate oxidase, and peroxidase) that produce a violet quinone monoimine dye with peak absorption at 550 nm. The method features zero-order reaction kinetics, provides a simple and rapid assay with an extended dynamic range, is specific and precise, gives results that correlate well (r greater than or equal to 0.99) with those of methods in which emulsified triolein is the substrate, and lends itself readily to automation. For all these reasons, the method seems highly suitable for routine use in clinical laboratories.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0009-9147
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Kinetic colorimetric assay of lipase in serum.
pubmed:affiliation
Research and Development Laboratory, Bayer Diagnostici SpA, Milan, Italy.
pubmed:publicationType
Journal Article, Comparative Study