Three hybridoma cell lines secreting antibodies against human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-OH-PGDH) were produced. Purified IgG2b from these cell lines recognized a distinct band of Mr 28,000 on SDS/PAGE from the purified enzyme as well as a band of Mr 56,000 from the crude enzyme preparation. These three monoclonal antibodies inhibited 15-OH-PGDH activity to different degrees. Inhibition of the enzyme activity could be prevented by prior incubation of the enzyme with NAD+ but not with prostaglandin E2 (PGE2) or NADP+. Inhibition by monoclonal antibodies appears to be non-competitive with respect to NAD+ and PGE2. An increased concentration of antibodies alters the apparent Km for NAD+ but not for PGE2, further supporting the notion that the antibodies bind to the coenzyme-binding site. The availability of these monoclonal antibodies should be valuable for probing the structure of the active site.
Research Article| April 01 1990
Monoclonal antibodies that inhibit the enzyme activity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase
C L Tai;
O T Mak;
Biochem J (1990) 267 (1): 75–78.
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C L Tai, O T Mak, T Arai, H H Tai; Monoclonal antibodies that inhibit the enzyme activity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochem J 1 April 1990; 267 (1): 75–78. doi: https://doi.org/10.1042/bj2670075
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