[A practical enzymatic cholesterol determination].
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Cholesterol↗
Biomedical subjects
K Stinshoff
Publications and source records attributed to K Stinshoff.
Relation between concentrations of free glycerol and triglycerides in human sera.
The concentrations of total glycerol, unesterified glycerol, and glycerol deriving from triglycerides (triacylglycerols) were measured in 468 fresh human sera from unselected outpatients of a municipal hospital. The distribution mode of free glycerol was log-normal; that of triglycerides was neither normal nor log-normal. A weak but statistically approved correlation between these variables was demonstrated. A comparison of triglyceride concentrations corrected for unesterified glycerol with those based on total glycerol shows that, for the triglycerides determination, analysis for total glycerol and substraction of 0.11 mmol/liter from the resulting value appears to be justified in clinical routine. Subtraction of individual sample-blank values is unnecessary. In a triglyceride concentration range from 1.71 to 2.85 mmol/liter the 95 percentile for the possible error of this procedure ranges from + 0.04 to - 0.08 mmol/liter.
Glycerol↗
Comparison of the cerebroside sulphatase and the arylsulphatase activity of human sulphatase A in the absence of activators.
A cerebroside sulphatase (cerebroside-3-sulphate 3 sulphohydrolase, EC 3.1.6.8) assay based on radio thin-layer chromatography is described. The substrate was labelled by the catalytic addition of tritium to cerebroside sulphate. Using this assay the cerebroside sulphatase activity of sulphatase A (Aryl-sulphate sulphohydrolase, EC 3.1.6.1) from human liver and kidney in the absence of activators was investigated. The pH optimum of this reaction depends on the buffer concentration, being pH 4.5 at 50 mM and 5.3 at 10 mM sodium formate. With the latter concentration the apparent Km for cerebroside sulphate is 0.06 mM; SO2-4 and nitrocatechol sulphate inhibit noncompetitively with a Ki of 4.51 mM for Na2SO4 and 0.43 mM for nitrocatechol sulphate. The cerebroside sulphatase activity of sulphatase A is highly dependent on the ionic strength. The optimum sodium formate concentration is 10 mM, and the cerebroside suophatase activity decreases rapidly with increasing buffer concentration. The same concentration dependence is observed in the inhibitory effect of cerebroside sulphate on the arylsulphatase reaction. The inhibition decreases at increasing buffer concentrations, becoming an activation at 70 mM sodium formate. The progress curve of the cerebroside sulphatase reaction shows a deviation from linearity similar to that of the arylsulphatase reaction. Investigation of the effect of preincubation with cerebroside sulphate on the arylsulphatase activity of the enzyme shows that cerebroside sluphatase activity and inactivation of the enzyme by cerebroside sulphate occur simultaneously. These observations are interpreted as supporting the assumption that cerebroside suophate and arylsulphates are degraded at an identical active site on the same enzyme. Differences in the properties of the cerebroside sulphatase and the arylsulphatase reaction of the enzyme may be attributed to the differences in the physiocochemical state of the two substrates.
Binding Sites↗