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Tamm-Horsfall urinary glycoprotein. The chemical composition
The Biochemical Journal
|November 1, 1970
Summary
This study details the amino acid and carbohydrate composition of Tamm-Horsfall glycoprotein, finding no significant differences in cystic fibrosis patients. The glycoprotein has high half-cystine content and lacks detectable thiol or N-terminal amino acids.
Area of Science:
- Biochemistry
- Glycoprotein analysis
- Human physiology
Background:
- Tamm-Horsfall glycoprotein (THG) is a major urinary glycoprotein.
- Understanding its composition is crucial for physiological and pathological studies.
Purpose of the Study:
- To present a revised amino acid and carbohydrate composition of human Tamm-Horsfall glycoprotein.
- To investigate potential compositional differences in THG from cystic fibrosis patients.
Main Methods:
- Amino acid analysis
- Carbohydrate composition analysis
- Performic acid oxidation
- S-alkylation with iodoacetate and iodoacetamide
- Alkaline treatment to assess glycosidic linkages
Main Results:
- Revised amino acid and carbohydrate composition of human THG.
- No significant differences in amino acid composition were found in THG from cystic fibrosis patients.
- High half-cystine content (1 per 11-12 residues) confirmed; no free thiol groups detected.
- Predominant carbohydrate-protein linkages are likely not O-glycosidic.
- No N-terminal amino acid was detected.
Conclusions:
- The study provides a detailed compositional profile of human Tamm-Horsfall glycoprotein.
- Cystic fibrosis does not appear to alter the amino acid composition of THG.
- The structural analysis suggests specific linkage types within the glycoprotein.
