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Characterization of a novel monoclonal antibody that senses nitric oxide‐dependent activation of soluble guanylate cyclase
Author(s) -
Tsuyama Shingo,
Yamazaki Eri,
Tomita Takeshi,
Ihara Hideshi,
Takenaka Shigeo,
Kato Keiko,
Kozaki Shunji
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00884-4
Subject(s) - monoclonal antibody , guanylate cyclase , gucy1a3 , chemistry , nitric oxide , gucy1b3 , microbiology and biotechnology , protein subunit , antibody , enzyme , biochemistry , guanylate cyclase 2c , biology , immunology , organic chemistry , gene
Two monoclonal antibodies (mAbs) against bovine lung soluble guanylate cyclase (sGC) were prepared and characterized. mAb 3221 recognized both the α‐ and β‐subunits of sGC and had greater binding affinity to the enzyme in the presence of NO. mAb 28131 recognized only the β‐subunit and its affinity did not change with NO. Neither mAb cross‐reacted with particulate GC. Cultured Purkinje cells from rats were treated with S ‐nitroso‐ N ‐acetylpenicillamine, an NO donor, and examined by immunocytochemical methods. The immunoreactivity associated with mAb 3221 increased with the cGMP content in a crude extract of cerebellum and the NO 2 generated in the culture medium increased.