Online citations, reference lists, and bibliographies.

A Fluorometric Assay For L-asparaginase Activity And Monitoring Of L-asparaginase Therapy.

P. Ylikangas, I. Mononen
Published 2000 · Chemistry, Medicine

Cite This
Download PDF
Analyze on Scholarcy
Share
The antineoplastic enzyme L-asparaginase is commonly used for the induction of remission in acute lymphoblastic leukemia (ALL). There is no simple method available for measuring the activity of this highly toxic drug. We incubated L-asparaginase from Erwinia chrysanthemi with L-aspartic acid beta-(7-amido-4-methylcoumarin) and measured the release of 7-amino-4-methylcoumarin fluorometrically for 30-300 min. The rate of the hydrolysis of the substrate was linear over a 50-fold range of the concentration of the enzyme. With increasing substrate concentration, the enzyme showed a saturable kinetic pattern with V(max) of 0.547 (SD 0.059) microM/min/mg of enzyme (n = 3) and Km of 0.302 (SD 0.095) mM (n = 3). This assay enables rapid analysis of L-asparaginase activity in biological samples and it can be used, for example, for monitoring of L-asparaginase activity in serum of ALL patients during their L-asparaginase therapy.
This paper references
10.1016/S0014-5793(97)00761-8
Recombinant human glycosylasparaginase catalyzes hydrolysis of l‐asparagine
T. Noronkoski (1997)
10.1006/abio.1993.1063
A fluorometric assay for glycosylasparaginase activity and detection of aspartylglycosaminuria.
I. Mononen (1993)
10.1016/0959-8049(96)00131-1
Monitoring of asparaginase activity and asparagine levels in children on different asparaginase preparations.
J. Boos (1996)
10.1080/10463356.1994.11904493
AHFS Drug Information
G. McEvoy (1994)
10.1016/S0003-2697(76)80066-8
A new fluorogenic substrate for chymotrypsin.
M. Zimmerman (1976)
10.1096/fasebj.7.13.8405810
Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation
I. Mononen (1993)
10.1038/bjc.1968.71
Factors which may influence the effectiveness of L-asparaginases as tumor inhibitors.
J. Broome (1968)
L-asparaginase II of Escherichia coli. Studies on the enzymatic mechanism of action.
M. Ehrman (1971)
Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase.
V. Kaartinen (1992)
10.1146/annurev.pa.10.040170.002225
L-Asparaginase and L-Asparagine Metabolism
Cooney Da (1970)
10.1248/cpb.38.153
An enzymatic method for the kinetic measurement of L-asparaginase activity and L-asparagine with an ammonia gas-sensing electrode.
S. Tagami (1990)
10.3109/10428199309149129
L-asparaginase and PEG asparaginase--past, present, and future.
M. Keating (1993)
10.1093/CLINCHEM/40.3.385
Enzymatic diagnosis of aspartylglycosaminuria by fluorometric assay of glycosylasparaginase in serum, plasma, or lymphocytes.
I. Mononen (1994)



This paper is referenced by
High-throughput asparaginase activity assay in serum of children with leukemia.
C. Fernandez (2013)
10.1097/FTD.0000000000000472
Therapeutic Drug Monitoring of Asparaginase Activity—Method Comparison of MAAT and AHA Test Used in the International AIEOP-BFM ALL 2009 Trial
C. Lanvers-Kaminsky (2018)
10.1109/ICAE.2011.5943923
A PPY/PT for assaying L-asparaginase activity in Proteus vulgaris the construction and application of the piezoelectric transducer
Jiali Ren (2011)
10.1080/07388550601173926
L-Asparaginase: A Promising Chemotherapeutic Agent
N. Verma (2007)
10.1007/s12010-015-1917-3
A Comprehensive Review on l-Asparaginase and Its Applications
T. Batool (2015)
10.1007/s00253-019-09890-0
Interferences that impact measuring optimal l-asparaginase activity and consequent errors interpreting these data
Marcela Medeiros de Freitas (2019)
10.1016/J.AB.2006.03.020
Enzyme-mediated individual nanoparticle release assay.
J. R. Glass (2006)
10.1016/j.jpba.2015.08.042
An analytical quality by design (aQbD) approach for a L-asparaginase activity method.
Han Min Yao (2016)
L-Asparaginase from Microbes: a Comprehensive Review
Devarai Santhosh Kumar (2012)
Research Article PRODUCTION OPTIMIZATION OF EXTRACELLULAR L-ASPARAGINASE THROUGH SOLID- STATE FERMENTATION BY ISOLATED BACILLUS SUBTILIS.
S. Shukla (2012)
10.1007/s00216-018-1326-x
A critical analysis of L-asparaginase activity quantification methods—colorimetric methods versus high-performance liquid chromatography
Agnes Magri (2018)
10.5897/AJB12.098
Antioxidant and antimicrobial efficacies of Amaranthus polygonoides and its impact on L-asparaginase production
Balakrishnan Naveena (2012)
10.1093/chromsci/bmy053
Optimization of a Precolumn OPA Derivatization HPLC Assay for Monitoring of l-Asparagine Depletion in Serum during l-Asparaginase Therapy.
Mei Zhang (2018)
10.1016/j.ab.2013.09.028
An Amplex Red-based fluorometric and spectrophotometric assay for L-asparaginase using its natural substrate.
C. S. Karamitros (2014)
10.1016/J.SNB.2009.12.006
The construction and application of a new PPY-MSPQC for l-asparaginase activity assay
Jiali Ren (2010)
10.1016/B978-0-444-63662-1.00012-9
Therapeutic Enzymes: l-Asparaginases
Jalaja Vidya (2017)
10.1016/j.biortech.2010.07.114
Purification and characterization of glutaminase-free L-asparaginase from Pectobacterium carotovorum MTCC 1428.
S. Kumar (2011)
10.1016/S0003-2697(02)00232-4
Analytical validation of a microplate reader-based method for the therapeutic drug monitoring of L-asparaginase in human serum.
C. Lanvers (2002)
10.1002/bmc.1096
An isocratic fluorescence HPLC assay for the monitoring of l-asparaginase activity and l-asparagine depletion in children receiving E. colil-asparaginase for the treatment of acute lymphoblastic leukaemia.
C. Nath (2009)
10.1016/j.blre.2020.100651
Critical overview of the main features and techniques used for the evaluation of the clinical applicability of L-asparaginase as a biopharmaceutical to treat blood cancer.
T A Costa-Silva (2020)
10.1016/S1367-5931(00)00184-8
Novel methods for biocatalyst screening.
D. Wahler (2001)
PRODUCTION OPTIMIZATION OF EXTRACELLULAR L-ASPARAGINASE THROUGH SOLID- STATE FERMENTATION BY ISOLATED BACILLUS SUBTILIS.
Susmita Mandal (2013)
10.1002/elsc.201700033
Ratiometric fluorescent l‐arginine and l‐asparagine biosensors based on the oxazine 170 perchlorate‐ethyl cellulose membrane
K. An (2017)
10.1097/00007691-200208000-00007
Serious Neutropenia in ALL Patients Treated With L-Asparaginase May Be Avoided by Therapeutic Monitoring of the Enzyme Activity in the Circulation
P. Ylikangas (2002)
10.1177/1082013209353219
Effect of Medium Composition and Kinetic Studies on Extracellular and Intracellular Production of L-asparaginase from Pectobacterium carotovorum
S. Arrivukkarasan (2010)
Research article PRODUCTION PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ANTI-LEUKAEMIC L-ASPARAGINASE FROM ISOLATED BACILLUS SUBTILIS USING SOLID STATE FERMENTATION.
Susmita Shukla (2013)
PRODUCTION PURIFICATION AND CHARACTERIZATION OF EXTRACELLULAR ANTI-LEUKAEMIC L-ASPARAGINASE FROM ISOLATED BACILLUS SUBTILIS USING SOLID STATE FERMENTATION
S. Shukla (2013)
10.20959/wjpps20175-9203
OVERVIEW ON L-ASPARAGINASE
Somavarapu Silpa (2017)
10.1039/C9AY00634F
Synthesis of surface imprinted core–shell nanospheres for the selective determination of asparaginase
Hebatallah A. Wagdy (2019)
10.1134/S0006297910030144
Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus
S. Bansal (2010)
10.1046/j.1471-4159.2003.01766.x
Gliap − a novel untypical l‐asparaginase localized to rat brain astrocytes
D. Dieterich (2003)
Semantic Scholar Logo Some data provided by SemanticScholar