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[Isolation and some properties of mink lysozyme]
Biokhimiia (Moscow, Russia)
|May 1, 1977
Summary
Mink lysozyme, isolated from spleen, kidney, and liver, exhibits a high histidine content and an unusual amino acid composition. Further analysis revealed a novel, bound component in the lysozyme preparations.
Area of Science:
- Biochemistry
- Enzymology
- Comparative Vertebrate Physiology
Context:
- Lysozyme (EC 3.2.1.17) is a crucial enzyme in innate immunity across various species.
- Investigating species-specific variations in lysozyme can reveal evolutionary adaptations and functional differences.
Purpose:
- To isolate and characterize lysozyme from mink (Mustela vison) tissues.
- To determine the amino acid composition and identify any unique properties of mink lysozyme.
- To investigate the presence of any associated components within the isolated lysozyme preparations.
Summary:
- Lysozyme was successfully isolated from mink spleen, kidney, and liver using affinity chromatography on deaminated chitin.
- Mink lysozyme demonstrates a notably high histidine content (7 residues/mole) and a balanced ratio of acidic to basic amino acids (20-22 residues each).
- The degree of amidation in mink lysozyme is relatively low (8-10%), and preparations contain an unidentified component absorbing light between 400-420 nm.
Impact:
- Provides foundational biochemical data on mink lysozyme, contributing to comparative enzymology.
- Highlights unique amino acid composition potentially linked to specific functional roles or evolutionary pressures in mink.
- The discovery of an unknown bound component warrants further investigation into its nature and potential biological significance.