Elestrostatic assay of phospholipase A activity: an application of the second harmonic method of monitoring membrane boundary potentials

Vladimir M. Mirsky, Vladimir V. Cherny, Valerij S. Sokolov, Vladislav S. Markin

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

To evaluate phospholipase A activity a new assay is suggested. This assay is based on the recording of boundary potential of the planar bilayer during enzymatic hydrolysis of lipids. To register these changes, a second harmonic method is used. Sensitivity of the assay is about 0.0002 units/ml regardless of the impurities that may be present in the samples. On eanalysis takes about 5 min.

Original languageEnglish (US)
Pages (from-to)277-284
Number of pages8
JournalJournal of Biochemical and Biophysical Methods
Volume21
Issue number4
DOIs
StatePublished - 1990

Fingerprint

Phospholipases A
Membrane Potentials
Assays
Hydrolysis
Membranes
Lipids
Monitoring
Enzymatic hydrolysis
Impurities

Keywords

  • Bilayer lipid membrane
  • Boundary
  • Enzyme assay
  • Phospholipase A
  • Surface potential

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

Cite this

Elestrostatic assay of phospholipase A activity : an application of the second harmonic method of monitoring membrane boundary potentials. / Mirsky, Vladimir M.; Cherny, Vladimir V.; Sokolov, Valerij S.; Markin, Vladislav S.

In: Journal of Biochemical and Biophysical Methods, Vol. 21, No. 4, 1990, p. 277-284.

Research output: Contribution to journalArticle

Mirsky, Vladimir M. ; Cherny, Vladimir V. ; Sokolov, Valerij S. ; Markin, Vladislav S. / Elestrostatic assay of phospholipase A activity : an application of the second harmonic method of monitoring membrane boundary potentials. In: Journal of Biochemical and Biophysical Methods. 1990 ; Vol. 21, No. 4. pp. 277-284.
@article{98f65b31aad54667af550e64095ea0fb,
title = "Elestrostatic assay of phospholipase A activity: an application of the second harmonic method of monitoring membrane boundary potentials",
abstract = "To evaluate phospholipase A activity a new assay is suggested. This assay is based on the recording of boundary potential of the planar bilayer during enzymatic hydrolysis of lipids. To register these changes, a second harmonic method is used. Sensitivity of the assay is about 0.0002 units/ml regardless of the impurities that may be present in the samples. On eanalysis takes about 5 min.",
keywords = "Bilayer lipid membrane, Boundary, Enzyme assay, Phospholipase A, Surface potential",
author = "Mirsky, {Vladimir M.} and Cherny, {Vladimir V.} and Sokolov, {Valerij S.} and Markin, {Vladislav S.}",
year = "1990",
doi = "10.1016/0165-022X(90)90002-T",
language = "English (US)",
volume = "21",
pages = "277--284",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",
number = "4",

}

TY - JOUR

T1 - Elestrostatic assay of phospholipase A activity

T2 - an application of the second harmonic method of monitoring membrane boundary potentials

AU - Mirsky, Vladimir M.

AU - Cherny, Vladimir V.

AU - Sokolov, Valerij S.

AU - Markin, Vladislav S.

PY - 1990

Y1 - 1990

N2 - To evaluate phospholipase A activity a new assay is suggested. This assay is based on the recording of boundary potential of the planar bilayer during enzymatic hydrolysis of lipids. To register these changes, a second harmonic method is used. Sensitivity of the assay is about 0.0002 units/ml regardless of the impurities that may be present in the samples. On eanalysis takes about 5 min.

AB - To evaluate phospholipase A activity a new assay is suggested. This assay is based on the recording of boundary potential of the planar bilayer during enzymatic hydrolysis of lipids. To register these changes, a second harmonic method is used. Sensitivity of the assay is about 0.0002 units/ml regardless of the impurities that may be present in the samples. On eanalysis takes about 5 min.

KW - Bilayer lipid membrane

KW - Boundary

KW - Enzyme assay

KW - Phospholipase A

KW - Surface potential

UR - http://www.scopus.com/inward/record.url?scp=0025009231&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025009231&partnerID=8YFLogxK

U2 - 10.1016/0165-022X(90)90002-T

DO - 10.1016/0165-022X(90)90002-T

M3 - Article

C2 - 2089069

AN - SCOPUS:0025009231

VL - 21

SP - 277

EP - 284

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

IS - 4

ER -