Investigation of Interaction Between Lactoferrin and Bio-Molecules

乳铁蛋白与生物分子相互作用的研究

• 批准号: 01560302
• 负责人: SHIMAZAKI Kei-ichi
• 金额: $ 0.96万
• 依托单位: Obihiro Univ. of AGR. & VET. MED.
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (C)
• 财政年份: 1989
• 资助国家: 日本
• 起止时间: 1989 至 1990
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-01560302/
• 关键词: Lactoferrin; Protein-Dye Complex; Isoelectric Point; Circular Dichroism Spectra; Interaction; Cibacron Blue; 円偏向二色性スペクトル; 等電点

The biological functions of lactoferrin have been characterized, such as its bacteriostatic effects, myelopoiesis, iron binding, and others. Therefore, The potential of utilization of lactoferrin in food, medicine and feed has remained the subject of intense investigation. It is supposed that one of the most fundamental functions of lactoferrin is the carrier of various ligands such as metals, drugs and other low molecular weight and high molecular weight substances. Thus, in this research project, the interacting properties of lactoferrin with dye, Cibacron blue F3GA, which is an analogous material of NAD or NADP, has been investigated by the spectrophotometric method. Cotton effect induced by the dye binding to lactoferrin was observed by circular dichroism spectra in the wavelength range between 250 and 400 nm. From this phenomenon. The number of dye bound to lactoferrin was estimatedto be 6 moles/mole. And this number was the same with both of apolactoferrin and iron-saturated lactoferrcn.On the other hand, the binding property of human lactoferrin against immobilized Cibacron blue was weaker than that of bovine lactoferrin. This difference may be due to the difference of pI values of bovine and human lactoferrins. Thus, both pI values of human and bovine lactoferrins were experimentally determined.

乳铁蛋白的生物学功能已被表征，例如其抑菌作用、骨髓生成、铁结合等。因此，乳铁蛋白在食品、药品和饲料中的利用潜力仍然是深入研究的课题。据认为，乳铁蛋白最基本的功能之一是各种配体如金属、药物和其他低分子量和高分子量物质的载体。因此，在本研究项目中，通过分光光度法研究了乳铁蛋白与染料 Cibacron blue F3GA（NAD 或 NADP 的类似材料）的相互作用特性。通过圆二色光谱在 250 至 400 nm 波长范围内观察到染料与乳铁蛋白结合诱导的棉花效应。从这个现象来看。与乳铁蛋白结合的染料数量估计为6摩尔/摩尔。并且这个数字与脱铁乳铁蛋白和铁饱和乳铁蛋白相同。另一方面，人乳铁蛋白对固定化Cibacron蓝的结合性能弱于牛乳铁蛋白。这种差异可能是由于牛和人乳铁蛋白的 pI 值不同所致。因此，人和牛乳铁蛋白的 pI 值都是通过实验确定的。

项目成果

K. Shimazaki and N. Nishio: "Affinity properties of tryptic fragments of bovine lactoferrin with immobilized Cibacron Blue F3GA" Jpn. J. Zootech. Sci.61(2). 169-171 (1990)

K. Shimazaki 和 N. Nishio：“牛乳铁蛋白胰蛋白酶片段与固定化 Cibacron Blue F3GA 的亲和力特性”Jpn。

K.Shimazaki and T.Hosokawa: "A tentative method for rapid preparation of ironsaturated lactoferrin by affinity chromotography" Animal. Sci. Technol.62. (1991)

K.Shimazaki 和 T.Hosokawa：“通过亲和色谱法快速制备铁饱和乳铁蛋白的尝试性方法”动物。

K.Shimazaki and T.Hosokawa: "A tentative method for rapid preparation of ironsaturated lactoferrin by affinity chromotography" Animal.Sci.Technol.62. (1991)

K.Shimazaki 和 T.Hosokawa：“通过亲和色谱法快速制备铁饱和乳铁蛋白的尝试性方法”Animal.Sci.Technol.62。

K.Shimazaki and N.Nishio: "Affinity properties of tryptic fragments of bovine lactoferrin with immobilized Cibacron Blue F3GA" Jpn.J.Zootech.Sci.61. 169-171 (1990)

K.Shimazaki 和 N.Nishio：“牛乳铁蛋白的胰蛋白酶片段与固定化 Cibacron Blue F3GA 的亲和力特性”Jpn.J.Zootech.Sci.61。

K.Shimazaki and N.Nishio: "Interacting properties of bovine lactoferrin with immobilized Cibacron Blue F3GA column" J.Dairy Sci.74. 404-408 (1991)

K.Shimazaki 和 N.Nishio：“牛乳铁蛋白与固定化 Cibacron Blue F3GA 柱的相互作用特性”J.Dairy Sci.74。