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Rabbit Tamm-Horsfall urinary glycoprotein. Chemical composition and subunit structure
The Biochemical Journal
|May 1, 1971
Summary
Researchers isolated and characterized Tamm-Horsfall glycoprotein from rabbit urine, revealing its carbohydrate content and subunit structure. Immunological studies showed cross-reactivity with human Tamm-Horsfall glycoprotein.
Area of Science:
- Biochemistry
- Urology
Background:
- Tamm-Horsfall glycoprotein (THG) is a major protein found in mammalian urine.
- Understanding the structure and properties of THG from different species can provide insights into its biological functions.
Purpose of the Study:
- To isolate and characterize Tamm-Horsfall glycoprotein (THG) from rabbit urine.
- To determine its chemical composition, subunit structure, and immunological properties.
Main Methods:
- Isolation and purification of THG using ultracentrifugation and electrophoresis.
- Chemical composition analysis (carbohydrate and amino acid content).
- Molecular weight determination using gel filtration and disc gel electrophoresis.
- N-terminal amino acid analysis.
- Immunological cross-reactivity studies.
Main Results:
- Homogeneous preparation of rabbit THG was obtained.
- THG contains approximately 31% carbohydrate, with amino acid composition similar to human THG.
- Leucine was identified as the sole N-terminal amino acid.
- The subunit molecular weight was determined to be approximately 84,000 +/- 6,000.
- Disulfide bonds were found to be intrachain.
- Immunological cross-reactivity was observed between rabbit and human THG.
Conclusions:
- Rabbit Tamm-Horsfall glycoprotein shares structural and immunological similarities with its human counterpart.
- This study provides a detailed characterization of rabbit THG, contributing to comparative studies of this important urinary protein.