• 제목/요약/키워드: Laptin

검색결과 2건 처리시간 0.016초

송엽(松葉)이 고지방식이(高脂肪食餌)로 유발된 백서(白鼠)의 지방(脂肪)과 혈청지질(血淸脂質)에 미치는 영향(影響)

  • 김대현;소경순
    • 대한약침학회지
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    • 제10권1호통권22호
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    • pp.109-119
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    • 2007
  • In order to study the effects of Pinus densiflora on hyperlipidemia and lipid in rats, we divided the rats into groups(Normal group, Control group and Sample group) and perfomed the experimental research. Hyperlipidemia and lipid in rats were induced by high fat diets for 8weeks. The sample group was administerd the extract of Pinus densiflora for 14 days and control group was administerd equal dose of oral. And then we measured the amount of serum triglyceride, Total cholesterol, LDL-cholesterol, HDL-cholesterol, Free Fatty Acid, phospholipid, Insuline, Laptin, Body weight, epididymis fat weight & rate, epididymis fat cell, Cardiac Risk Factor(CRF). The results were as followers : 1. Sample Group showed decreasing effects on Total cholesterol, Trigylceride, LDL-cholesterol, and Phospholipid levels in serum and CRF significantly. 2. Sample Group showed increasing effects on HDL-cholesterol level in serum significantly. 3. Sample Group showed decreasing effects on Insuline in serum significantly. 4. Sample Group showed increasing effects on Laptin in serum significantly. 5. Sample Group showed decreasing effects on Body weight, epididymis fat weight & rate, epididymis fat cell significantly. According to the above results, Pinus densiflora showed significant decreasing effects on hyperlipidemia and lipid in rats, it is considered that it is appropriate to apply for hyperlipidemia, obesity.

Secretory Production of Human Leptin in Bacillus subtilis

  • Jeong, Ki-Jun;Lee, Sang-Yup
    • Journal of Microbiology and Biotechnology
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    • 제10권6호
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    • pp.753-758
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    • 2000
  • Human leptin is identified as a 16kDa (146 amino acids) protein secreted from adipocytes which influences body weight homeostasis. In order to produce active leptin, the human obese gene coding for leptin was expressed in Bacillus subtilis WB600 strain which is deficient in six extracellular proteases. The recombinant leptin was produced in a culture supernatant, and in a culture supernatant, it was contained as high as 48% for total proteins. After simple purification steps, which consisted of ammonium sulfate precipitation and anion-exchange column chromatography, 2.3 mg of leptin with a purity greater than 95% was obtained from the 0.51 culture with the recovery yield of 38.3%. The purified leptin showed the correct folding structure with one disulfied bond.

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