Development of an Enzyme-Linked Immunosorbent Assay System for the Determination of Asymmetric Dimethylarginine Using a Specific Monoclonal Antibody
Author(s) -
Miyuki Yokoro,
Makiko Suzuki,
Machiko YATANI,
Hiromi Yamashita,
Yoshitaka Takahashi,
Hideaki Tsuji,
Masumi Kimoto
Publication year - 2012
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.110727
Subject(s) - asymmetric dimethylarginine , monoclonal antibody , chemistry , enzyme , arginine , nitric oxide synthase , antibody , microbiology and biotechnology , urine , non competitive inhibition , creatinine , monoclonal , nitric oxide , biochemistry , immunology , biology , amino acid , organic chemistry
We produced a monoclonal antibody (mAb) against N(G),N(G)-dimethyl-L-arginine (asymmetric dimethylarginine: ADMA), an endogenous competitive inhibitor of nitric oxide synthase (NOS), and developed an enzyme-linked immunosorbent assay (ELISA). The competitive ELISA method using the mAb determined 5 nM-100 nM ADMA, and ADMA levels in human plasma and urine were found to be 0.78 µM and 51.3 µmol/g of creatinine respectively.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom