Quantitation of phospholipase A2 and phospholipase C activity using alkaline phosphatase impregnated liposomes

Thomas B. Buxton, Brian Catto, Jack Horner, Rex Yannis, J. Peter Rissing

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Phospholipase A2 and C activity was quantitated using liposomes impregnated with alkaline phosphatase. Release of alkaline phosphatase was dependent on phospholipase related hydrolysis of intact vesicles. Released alkaline phosphatase was quantitated after addition of its chromogenic substrate p-nitrophenyl phosphate. The lower limit of detectability for phospholipase A2 and C activity was 0.5 unit/ml. These limits were 10-fold lower than a titrimetric method. Liposome destruction as measured by alkaline phosphatase release was calcium dependent and inhibited by 1 mM EDTA and 1 mM ZnSO4. The assay was technically simple, generated same day results, and used automated enzyme-linked immunosorbent assay instrumentation.

Original languageEnglish (US)
Pages (from-to)349-354
Number of pages6
JournalMicrochemical Journal
Volume34
Issue number3
DOIs
StatePublished - Jan 1 1986

Fingerprint

Phospholipases A2
Type C Phospholipases
Liposomes
Alkaline Phosphatase
Assays
Chromogenic Compounds
Immunosorbents
Phospholipases
Edetic Acid
Hydrolysis
Calcium
Enzymes

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy

Cite this

Quantitation of phospholipase A2 and phospholipase C activity using alkaline phosphatase impregnated liposomes. / Buxton, Thomas B.; Catto, Brian; Horner, Jack; Yannis, Rex; Rissing, J. Peter.

In: Microchemical Journal, Vol. 34, No. 3, 01.01.1986, p. 349-354.

Research output: Contribution to journalArticle

Buxton, Thomas B. ; Catto, Brian ; Horner, Jack ; Yannis, Rex ; Rissing, J. Peter. / Quantitation of phospholipase A2 and phospholipase C activity using alkaline phosphatase impregnated liposomes. In: Microchemical Journal. 1986 ; Vol. 34, No. 3. pp. 349-354.
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