Book ChapterDOI
21 Vertebrate Lysozymes
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This chapter focuses on vertebrate lysozymes, particularly hen egg-white (HEW) lysozyme, which is small and basic, and it separates well on weak acid resins, like Amberlite XE-64 or Bio-Rex 70 or carboxymethyl cellulose and on calcium phosphate gel.Abstract:
Publisher Summary This chapter focuses on vertebrate lysozymes, particularly hen egg-white (HEW) lysozyme. Lysozymes of other types generally are distinguishable from HEW lysozyme in having higher molecular weights and somewhat different enzymic activities. Lysozyme is small and basic, and it separates well on weak acid resins, like Amberlite XE-64 or Bio-Rex 70 or carboxymethyl cellulose and on calcium phosphate gel. Affinity chromatography of lysozyme has been carried out using dispersed chitin or carboxymethyl (CM)-chitin. The conditions required for elution from chitin columns suggest that there are two classes of adsorbent sites that are differently affected by pH and ionic strength in their interaction with the enzyme. The preparation of lysozyme from diverse animal sources is generally achieved in four main steps, which include (1) the preparation of a lysozyme-rich extract, (2) chromatography on CM-cellulose, (3) filtration on Sephadex G-25, and (4) ion exchange chromatography on Amberlite CG-50 at 20° C with a 0.2 M phosphate buffer. The chromatography is sensitive to the pH and small variation of no more than 0.1 pH unit can involve complete retention or exclusion.read more
Citations
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Journal ArticleDOI
Environment and exposure to solvent of protein atoms. Lysozyme and insulin.
A. Shrake,John A. Rupley +1 more
TL;DR: A computer program is described for calculating the environment and the exposure to solvent of atoms of a protein based on the atomic co-ordinates of the protein and on assumptions like those of Lee & Richards (1971).
Journal ArticleDOI
Aromatic contributions to circular dichroism spectra of proteins.
TL;DR: Aromatic Contributions To Circular Dichroism Spectra Of Protein this paper were discussed in detail in the CRC Critical Reviews in Biochemistry: Vol. 2, No. 1, pp. 113-175.
Journal ArticleDOI
Tapping the immunological repertoire to produce antibodies of predetermined specificity
TL;DR: This work has shown that chemically synthesized peptides representative of virtually any part of the surface of a protein can elicit antibodies reactive with the native molecule, and antibodies, useful in the study of changes in protein structure, can be generated.
Journal ArticleDOI
Helix to helix packing in proteins
TL;DR: Analysis of the pattern of residue to residue contacts at the interface of 50 helix to helix packings observed in ten proteins of known structure supports a model for helix-to- helix packing in which the ridges and grooves on the helix surface intercalate.
Journal ArticleDOI
Detection of transient protein folding populations by mass spectrometry.
TL;DR: Electrospray ionization mass spectrometry has been used to obtain the distribution of masses within a population of protein molecules that had undergone hydrogen exchange in solution, helping to detail the pathways available to a protein during refolding.
References
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Journal ArticleDOI
A general method applicable to the search for similarities in the amino acid sequence of two proteins
TL;DR: A computer adaptable method for finding similarities in the amino acid sequences of two proteins has been developed and it is possible to determine whether significant homology exists between the proteins to trace their possible evolutionary development.
Journal ArticleDOI
The interpretation of protein structures: estimation of static accessibility.
B. Lee,Frederic M. Richards +1 more
TL;DR: The accessibility of atoms in the twenty common amino acids in model tripeptides of the type Ala-X-Ala are given for defined conformation and the larger non-polar amino acids tend to be more “buried” in the native form of all three proteins.
Book ChapterDOI
Some factors in the interpretation of protein denaturation.
TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Journal ArticleDOI
Computed circular dichroism spectra for the evaluation of protein conformation
Journal ArticleDOI
Spectroscopic determination of tryptophan and tyrosine in proteins.
TL;DR: A procedure is presented which strongly reduces or elimi- nates these interactions, normalizes their absorption, and consequently permits a more precise analysis of tryptophan and tyrosine in proteins.