Influence of Monoethanolamine on Activity Measurements of the Isoenzymes of Alkaline Phosphatase

Jung, Klaus; Pergande, M; Reichmann, G.; Sitte, Astrid; Egger, E

doi:10.1515/cclm.1978.16.4.223

Cited by 4 publications

(3 citation statements)

References 7 publications

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“…As in DEA buffer, there is sufficient stability for the clinically relevant isoenzymes from bones and liver. It is known that already low concentrations of monoethanolamine in DEA buffer lead to an inhibition of AP activity (2, 17) and that indi vidual isoenzymes are concerned to different extents (9), and thus this buffer has been re jected again. The AMPD buffer, therefore, could be a good alternative for AP activity determinations at 37 °C.…”

Section: Discussionmentioning

confidence: 99%

Stability of Isoenzymes of Alkaline Phosphatase in Various Buffer Systems

Jung¹,

Pergande²,

Egger³

1979

Enzyme

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The stability of isoenzymes of alkaline phosphatase from liver, bones and small intestine was compared after addition to inactivated serum in the buffer systems: glycine, 2-amino-2-methyl-l-propanol, diethanolamine and 2-amino-2-methyl-l ,3-propandiol at 37 °C. The mentioned isoenzymes were inactivated to different extents in glycine and 2-amino-2-methyl-lpropanol buffers. In diethanolamine and 2-amino-2-methyl-l ,3-propandiol buffers sufficient stability of isoenzymes is obtained so that only these buffers are suitable for activity determinations of alkaline phosphatase at 37 °C.

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Section: Discussionmentioning

confidence: 99%

Stability of Isoenzymes of Alkaline Phosphatase in Various Buffer Systems

Jung¹,

Pergande²,

Egger³

1979

Enzyme

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“…This holds pri marily for the purity of the buffer used and the amount of inorganic phosphate and 4-nitrophenol in the substrate 4-nitrophenylphosphate [24][25][26]. From studies of Simpson et al [26] and from Jung and Pergande [27] it is obvious that especially placental phospha tase is inhibited by inorganic phosphate, present as an impurity in the reagents.…”

Section: Discussionmentioning

confidence: 99%

Stability Test of Six Enzymes for Internal Quality Control

Hafkenscheid¹,

Ven-Jongekrijg²

1983

Enzyme

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The daily quality control for the determination of the catalytic activity concentrations of enzymes is an important aspect in clinical chemistry. Instead of the expensive, commercially available control sera, we have looked for a simple, reliable and cheap method for the quality control of enzyme determinations. Commercially available enzymes were suspended in an albumin solution and ampoules were filled with 1.0 ml of these various solutions. The ampoules were stored at 4 °C or-20 °C. Once a week, during 10 months, catalytic activities of these enzyme-albumin solutions were determined together with the same activities in freshly reconstituted control sera. Aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, creatine kinase and y-glutamyltransferase were determined at 30 °C according to well-described methods. a-Amylase was determined with the Phadebas method at 37 °C. Except for creatine kinase, the stability and reliability of these enzyme solutions are fully comparable with control sera during the experimental period. The catalytic activity concentration of creatine kinase decreased slowly during the 10 months. The enzyme solutions react in the same manner as commercial test sera on changes in the reaction conditions for the enzyme determinations. The conclusion seems justified that these enzyme solutions can be used for the daily quality control of the enzyme determinations instead of control sera.

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“…in diethanolamine both display a positive bias versus isoenzymes present in sera of healthy people and those of intestinal and placental origin (1). Both aminoalcohols often contain inactivating impurities as 5-amino-3-aza-2,2,5-trimethylhexanol (6) in 2amino-2-methyl-l-propanol, and monoethanolamine (7) in diethanolamine. Therefore, we evaluated the use of methylglucamine, a pure buffer substance with moderate phosphate-acceptor properties, which has been proposed by Chromy et al (8) for alkaline phosphatase determination and recommended by the Italian society (9).…”

Section: Introductionmentioning

confidence: 99%

Technical report

1992

Clinical Chemistry and Laboratory Medicine

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Influence of Monoethanolamine on Activity Measurements of the Isoenzymes of Alkaline Phosphatase

Cited by 4 publications

References 7 publications

Stability of Isoenzymes of Alkaline Phosphatase in Various Buffer Systems

Stability of Isoenzymes of Alkaline Phosphatase in Various Buffer Systems

Stability Test of Six Enzymes for Internal Quality Control

Technical report

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