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Molecular characterization of 20 alpha‐HSD gene during bovine estrus cycle
Author(s) -
Min KwanSik,
Naidansuren P.,
Park J.J.,
Yun S.J.,
Kang Y.S.,
Kang Y.S.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.518.2
Subject(s) - corpus luteum , estrous cycle , ovary , placenta , biology , western blot , messenger rna , ovulation , microbiology and biotechnology , andrology , medicine , endocrinology , fetus , gene , pregnancy , biochemistry , hormone , genetics
The enzyme 20a‐hydroxysteroid dehydrogenase catalyzes the conversion of proesterone into its inactive form, 20a‐hydroxyprogesterone.Bovine ovary of corpus luteum were obtained at the slaughter. Placenta was also obtained at laparotomy under general anesthesia from a somatic cell nuclear transfer on day 280 of gestation. We determined the expression pattern of 20a‐hydroxysteroid dehydrogenase mRNA and protein by the real‐time polymerase chain reaction, northern, western blot, immunohistochemistry and immuno Flourescence. The mRNA and protein expression was highly detected in the corpus luteum 1 stage ovary. The molecular weight of rec‐protein produced in animal cells was founded in about 37 kDa by the expression vector pcDNA3aHSD. Thus, it may be could understand the function and role of bovine physiology during estrus cycle (ovulation mechanism), pregnancy and parturiton. This grant was from BioGreen 21 program (#20080401034074), Rural Developmental Administration, Republic of Korea.