• Journal of Dairy Science and Biotechnology
• /
• 제27권1호
• /
• pp.19-28
• /
• 2009

Lactoferrin was first identified 60 years ago as a "red protein" in bovine milk. Lactoferrin, one of the transferrin family proteins, is an iron-binding glycoprotein found in milk and various mucosal secretions; it is also released from activated neutrophils. Human lactoferrin has a molecular weight of 82.4 kDa and is composed of 702 or 692 amino acid residues. Bovine lactoferrin has a molecular weight of 83.1 kDa and is composed of 689 amino acid residues. Both lactoferrin and transferrin have the ability to bind two $Fe^{3+}$ ions, together with two ${CO_3}^{2-}$ ions with extremely high affinity; these proteins also have the ability to release this iron at low pH levels. The polypeptide chain in lactoferrin is folded into two globular lobes, representing the N-terminal and C-terminal halves. Both lobes have similar folding and 40% sequence identity. This protein is capable of multiple functions as described in various review papers, including antimicrobial, antiviral, antiinflammatory, anticancer, antioxidant, and cell growth-promoting activities. Lactoferrin also exhibits immunomodulating effects and plays an active role in the regulation of myelopoiesis and the inhibition of bacterial translocation.

• 한국축산식품학회지
• /
• 제28권4호
• /
• pp.408-414
• /
• 2008

본 연구에서 제조한 저지방 훈연 소시지는 활성락토페린을 각각 0, 0.3 및 0.6%로 함량을 달리하였고, 냉장저장($8^{\circ}C$)중 이화학적 및 조직학적 특성과 접종 미생물의 성장에 미치는 영향을 조사하기 위해 실시하였다 제조된 저지방 훈연소시지의 pH, 수분, 지방, 및 단백질의 함량은 각각 6.04-6.08, 72-76%, 1-2%, 12-14%로 처리구별 유의적인 차이가 없었다(p>0.05). 활성락토페린을 0.6% 첨가한 처리구는 0.3% 첨가구와 달리 무첨가 대조구에 비해 미생물의 성장을 억제하였으며(p<0.05), 유의적으로 높은 부서짐성을 보였다. 그러나 젖산나트륨 3.3%를 첨가에 의한 항균활성 효과보다는 낮은 효과로 평가되었다. 이상의 결과를 종합해 본 결과 락토페린은 육제품에 있어서 이화학적 및 조직학적성상에 거의 영향을 주지 않으면서 항균활성을 부여하는 좋은 기능성 물질로서 이용할 수 있을 것으로 판단된다.

• Journal of Periodontal and Implant Science
• /
• 제23권1호
• /
• pp.48-55
• /
• 1993

Macrophage inflammatory $protein-1{\alpha}(MIP-1{\alpha})$ from activated T cell or macrophage, which is small inducible cytokine of unkown biological function, has been shown to display inflammation chemokinetic activities, as well as myelosuppressive effect on more immature progenitor cells. In this paper we show the $MIP-1{\alpha}$ mRNA expression and the presence of $MIP-1{\alpha}$ binding sites from murine macrophage cell line RAW 264.7, and primary cells of mouse bone marrow and spleen. $MIP-1{\alpha}$ mRNA was induced from LPS-stimulated RAW 264.7, but not inhibited by cyclosporin A treatment, and also was expressed from mouse splenocyted and bone marrow cell which were not increased by ferritin or lactoferrin treatment. The results of receptor binding assay showed that radiolabeled RAW 264.7 cell with kd value of 0.91 nM, and binding sites per cell of 378. bone marrow cell and splenocyte also appeared to have $MIP-1{\alpha}$ binding sites 33 and 11 per cell, respectiviely.