Autor: |
Kanevsky VYu; Moscow Research Institute of a Medical Ecology, Russia., Pozdnyakova LP, Katukov VYu, Severin SE |
Jazyk: |
angličtina |
Zdroj: |
Biochemistry and molecular biology international [Biochem Mol Biol Int] 1997 Jun; Vol. 42 (2), pp. 309-14. |
DOI: |
10.1080/15216549700202701 |
Abstrakt: |
The transferrin receptor (TFR) has been detected in tissues characterised by a high degree of proliferation. We have developed a procedure for isolating TFR from human placental tissues by affinity chromatography on transferrin-Sepharose. Using gel filtration and electrophoresis in 7% PAAG, it has been shown that the molecular mass of the protein is 180 kDa. The protein has a subunit structure and is made up of two identical subunits, 90 kDa each. The constant for the protein binding to transferrin is equal to 5 x 10(-9) M. The yield of the protein isolated by the novel procedure exceeds 5-fold that obtained by previously described methods. |
Databáze: |
MEDLINE |
Externí odkaz: |
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