Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-9-28
pubmed:abstractText
Phenosulphotransferase (EC 2.8.2.1) (PST) is an important catecholamine and drug metabolizing enzyme. Optimal conditions have been determined for the accurate measurement of PST activity in the human platelet, human renal cortex, and human jejunum with a radiochemical microassay. 3-Methoxy-4-hydroxyphenylglycol (MHPG) and 35S-3'-phosphoadenosine-5'-phosphosulfate (35S-PAPS) were the substrates for the reaction. The apparent Michaelis-Menten (Km) values for MHPG with platelet, renal cortex, and jejunum were 1.09, 0.46 and 1.16 mmol/l, respectively. Apparent Km values for PAPS in the same tissues were 0.14, 0.13 and 0.21 mumol/l. The pH optimum of the reaction in all three tissues was approximately 6.2--6.8 with three different buffer systems. The coefficients of variation for the assay of platelet, renal cortex, and jejunal activities were 6.2%, 3.4% and 4.4%, respectively. Mean platelet PST activity in blood samples from 75 randomly selected adult subjects was 5.0 +/- 1.72 nmol of MHPG sulfate formed per hour per mg of platelet protein (8.3 x 10(-5) +/- 2.9 x 10(-5) mumol . min-1 . mg-1, mean +/- S.D.). There was a 5-fold intersubject variation in platelet PST activity within two standard deviations of the mean value. Experiments in which partially purified human erythrocyte PST was added to platelet, kidney and gut homogenates under these assay conditions provided evidence that endogenous PST inhibitors did not affect the observed enzyme activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Phenolsulphotransferase in human tissue: radiochemical enzymatic assay and biochemical properties.
pubmed:publicationType
Journal Article