• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.2
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• pp.251-255
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• 2008

Cholesterol and cholesterol oxide products (COPs) of Gulbi (Pseudosciaena manchurica) processed and stored at different salting times of 5 hours and 5 days were analyzed. The content of cholesterol was $133.4{\pm}5.20\;mg/100\;g$ in the fresh sample. Cholesterol content was decreased during salting and storage; its contents were $130.3{\pm}2.95\;mg/100\;g$ and $87.2{\pm}3.49\;mg/100\;g$ in 5 hours and 5 days salting samples, respectively. The content of 7-ketocholesterol in 5 hours and 5 days salting samples were $75.2{\pm}2.70\;{\mu}g/100\;g$ and $82.4{\pm}3.30\;{\mu}g/100\;g$. The 7-ketocholesterol content of salting sample for 5 hours had no significantly difference for 2 days sun drying, but it was dramatically increased during 5 days sun drying and then increased during storage days. $7{\alpha}-$ and $7{\beta}-hydroxycholesterol$ were not detected in fresh sample, but increased during Gulbi processing and storage. The $7{\alpha}-hydroxycholesterol$ was increased during Gulbi processing and storage and a higher level of $658.1{\pm}6.20\;{\mu}g/100\;g$ was detected in 5 hours salting sample than in 5 days salting sample after 21 days storage. The $7{\beta}-hydroxycholesterol$ also showed similar tendency with $7{\alpha}-hydroxycholesterol$; it was largely increased between 7 and 14 days storage in 5 days salting sample.

• Journal of Life Science
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• v.34 no.2
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• pp.86-93
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• 2024

Since replication of plasmids must be strictly controlled, plasmids that generally perform rolling circle replication generally maintain a constant copy number by strictly controlling the replication initiator Rep at the transcriptional and translational levels. Plasmid pJB01 contains three orfs (copA, repB, repC or repABC) consisting of a single operon. From analysis of amino acid sequence, pJB01 CopA was homologous to the Cops, as a copy number control protein, of other plasmids. When compared with a CopG of pMV158, CopA seems to form the RHH (ribbon-helix-helix) known as a motif of generalized repressor of plasmids. The result of gel mobility shift assay (EMSA) revealed that the purified fusion CopA protein binds to the operator region of the repABC operon. To examine the functional role of CopA on transcriptional level, 3 point mutants were constructed in coding frame of copA such as CopA R16M, K26R and E50V. The repABC mRNA levels of CopA R16M, K26R and E50V mutants increased 1.84, 1.78 and 2.86 folds more than that of CopA wt, respectively. Furthermore, copy numbers owing to mutations in three copA genes also increased 1.86, 1.68 and 2.89 folds more than that of copA wt, respectively. These results suggest that CopA is the transcriptional repressor, and lowers the copy number of pJB01 by reducing repABC mRNA and then RepB, as a replication initiator.