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The molecular components of human transferrin type C.
International Journal of Peptide and Protein Research
|January 1, 1977
Summary
Human transferrin type C (TfC) exhibits heterogeneity with three components (A, B, C) differing in sialic acid content. This multiplicity is likely due to biosynthesis, not sialic acid loss in circulation.
Area of Science:
- Biochemistry
- Proteomics
- Human Physiology
Background:
- Human transferrin type C (TfC) is a key iron transport protein.
- Previous studies suggested heterogeneity within TfC, but the underlying reasons were unclear.
Purpose of the Study:
- To investigate the heterogeneity of immunologically pure human transferrin type C (TfC).
- To determine the chemical basis for TfC component multiplicity.
- To explore the biosynthetic origin of TfC heterogeneity.
Main Methods:
- Isolation of TfC from healthy donors.
- Analysis using polyacrylamide gel electrophoresis and DEAE-cellulose chromatography.
- Sialic acid content determination and baboon transferrin analysis.
Main Results:
- TfC resolved into three components (A, B, C) with varying sialic acid content (A
- Iron binding did not influence chromatographic resolution.
- No significant differences were observed in TfC from patients with liver disease compared to healthy individuals.
- Baboon transferrin showed similar sialic acid heterogeneity, with no age-dependent differences.
Conclusions:
- The heterogeneity of TfC is primarily attributed to variations in sialic acid content.
- The observed multiplicity of TfC is likely a result of the biosynthetic process, rather than post-circulatory modification.
- TfC heterogeneity is not linked to liver disease in the studied patients.