Immobilization of an Esterase Inhibitor on a Porous Hollow-Fiber Membrane by Radiation-Induced Graft Polymerization for Developing a Diagnostic Tool for Feline Kidney Diseases

Removal of the major urinary protein, cauxin, a carboxylesterase, from cat urine is essential for distinguishing between physiological and abnormal proteinuria by a urine dipstick. We have previously developed a material for removing cauxin by using lens culinaris agglutinin (LCA) lectin which targe...

Full description

Saved in:
Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2013, Vol.77 (10), p.2061-2064
Main Authors: MATSUNO, Shinya, UMENO, Daisuke, MIYAZAKI, Masao, SUZUTA, Yasuyuki, SAITO, Kyoichi, YAMASHITA, Tetsuro
Format: Article
Language:English
Subjects:
Acetone - analogs & derivatives
Acetone - chemistry
Acetone - pharmacology
Animals
carboxylesterase
Carboxylesterase - chemistry
Carboxylesterase - isolation & purification
Carboxylesterase - urine
Cat Diseases - diagnosis
Cat Diseases - urine
Cats
cauxin
Chains (polymeric)
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
esterase inhibitor
Esterases
Esterases - antagonists & inhibitors
Grafting
Inhibitors
kidney disease
Kidney diseases
Kidney Diseases - diagnosis
Kidney Diseases - urine
Lectins
Lens culinaris
Ligands
Male
Membranes
Membranes, Artificial
Polymerization
Porosity
radiation-induced graft polymerization
Sulfides - chemistry
Sulfides - pharmacology
Urine
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Removal of the major urinary protein, cauxin, a carboxylesterase, from cat urine is essential for distinguishing between physiological and abnormal proteinuria by a urine dipstick. We have previously developed a material for removing cauxin by using lens culinaris agglutinin (LCA) lectin which targets the N-linked oligosaccharides present in cauxin. To improve the affinity and specificity toward cauxin, we immobilized 1,1,1-trifluoro-3-(2-sulfanylethylsulfanyl) propane-2-one, an inhibitor of esterases, to a polymer chain grafted on to a porous hollow-fiber membrane by applying radiation-induced graft polymerization. Normal male urine was forced to permeate through the pores rimmed by the ligand-immobilized polymer chain. Cauxin could not be detected in the effluent from the membrane. The residence time of the urine across a membrane thickness of 1 mm was set at 7 s. The respective dynamic and equilibrium binding capacities of the membrane for cauxin were 2 and 3 mg/g. The developed cauxin-affinity membrane material was more effective for diagnosing cat kidney diseases than the LCA lectin tip.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.130428