Comparative studies on the interaction of various transferrins and rat bone marrow cells. |
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| Authors: | N J Verhoef H C Kester P J Noordeloos B Leijnse |
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| Affiliation: | 1. College of Civil Engineering, Hunan University, Changsha, Hunan 410082, China;2. Faculty of Heat & Refrigeration Engineering, Industrial University of Ho Chi Minh City, Ho Chi Minh 700000, Viet Nam;3. Division of Computational Mathematics and Engineering, Institute for Computational Science, Ton Duc Thang University, Ho Chi Minh City, Viet Nam;4. Faculty of Civil Engineering, Ton Duc Thang University, Ho Chi Minh City, Viet Nam;5. Faculty of Information Technology, Industrial University of Ho Chi Minh City, 700000, Viet Nam |
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| Abstract: | - 1.1. The affinity of bovine transferrin for receptor sites on cell membranes of rat bone marrow cells was found to be much lower than of rat or human transferrin.
- 2.2. The apparent Michaelis constant for rat transferrin and bovine transferrin appeared to be 1.25 × 10−6 and 3.2 × 10−6mol/l, respectively.
- 3.3. The apparent Michaelis constant for rat transferrin was independent on its iron saturation. The binding at equilibrium of [125I]labelled rat transferrin to rat bone marrow cells varied only slightly with the iron saturation of transferrin.
- 4.4. Rat diferric- and monoferric-transferrin had the same affinity for rat bone marrow cell receptors.
- 5.5. The affinity of rat apotransferrin for these receptors was about one half of those of diferricand monoferric-transferrin.
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