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Book ChapterDOI

[83] Purification of native and synthetic lysozyme with (tri-(N-acetylglucosamine)-agarose

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TLDR
The preparation and use of an affinity adsorbent based on a low molecular weight substrate analog of lysozyme, which could be used for coupling other saccharides to agarose is described.
Abstract
Publisher Summary Affinity chromatography of lysozyme has been carried out using a variety of adsorbents: dispersed chitin, carboxymethylated chitin, deaminated chitin, and chitin-coated cellulose. This chapter describes the preparation and use of an affinity adsorbent based on a low molecular weight substrate analog of lysozyme. The procedure for preparation of the adsorbent is general and could be used for coupling other saccharides to agarose. The experiments described in this chapter were carried out in order to determine optimum elution conditions for handling small amounts of lysozyme such as are manipulated during purification of synthetic protein.

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Citations
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Journal ArticleDOI

Egg White Lysozyme Purification by Ultrafiltration and Affinity Chromatography

TL;DR: Isolation and purification of lysozyme from hen egg white was studied using a two-step procedure and the overall lyso enzyme recovery was 79%.
Journal ArticleDOI

Optical properties of lysozyme. pH and saccharide binding difference spectra.

TL;DR: Perturbation of Trp-108 and one or more other tryptophan residues by several carboxylate groups is responsible for the low pH difference spectra of the unliganded HEW and TEW lysozyme molecules.
Journal ArticleDOI

Oxindolealanine-62 lysozyme: equilibrium, calorimetric, and kinetic studies of the reaction with N-acetylglucosamine oligosaccharides.

Andrew Shrake, +1 more
- 19 Aug 1980 - 
TL;DR: The results indicate that the interactions of the ABC region of the active site with substrates are substantially altered by Trp-62 oxidation, more than expected for loss only of the TrP-62 interactions.
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