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Journal ArticleDOI

Physicochemical properties of β-casein and some carboxyacyl derivatives

M.T.A. Evans, +2 more
- 16 Feb 1971 - 
- Vol. 229, Iss: 2, pp 411-422
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TLDR
The effect of carboxyacylation on the aggregation and conformation of β-casein A has been examined by ultracentrifugation and optical rotatory dispersion.
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This article is published in Biochimica et Biophysica Acta.The article was published on 1971-02-16. It has received 25 citations till now. The article focuses on the topics: Optical rotatory dispersion & Succinylation.

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Citations
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Journal ArticleDOI

Nomenclature of Proteins of Cow's Milk: Fifth Revision

TL;DR: Because of increased interest in milk proteins of species other than bovine, the Committee suggests that these be identified as homologs of those already characterized in European, Bos taurus , and Indian, Bos indicus , cattle.
Book ChapterDOI

Chemistry of the caseins.

TL;DR: The caseins have been inaccurately classified as denatured or random coil proteins as mentioned in this paper, since they appear more flexible and less stable than typical globular or rod-shaped proteins, they appear to have some secondary structure and a definite unordered tertiary structure.
Journal ArticleDOI

Nomemclature of the proteins of cow's milk: fourth revision.

TL;DR: It is recommended that their behavior in gel electrophoresis under suitable conditions be employed for this purpose for all of the "major" milk proteins of raw skim milk except the immunoglobulins where, because of their heterogeneity and molecular genetics, physical parameters are less useful and their identification must be based upon antigenic determinants and their homology with their human counterparts.
Book ChapterDOI

Proteins of Milk

TL;DR: The proteins of milk are of great importance in human nutrition and influence the behavior and properties of the dairy products containing them as mentioned in this paper, and they have been studied more extensively than any other proteins except possibly those of blood.
Journal ArticleDOI

The conformation and aggregation of bovine β‐casein A. I. Molecular aspects of thermal aggregation

TL;DR: The conformation of β-casein A in the monomeric and thermally aggregated states has been investigated by a range of techniques as discussed by the authors, and β-Casein A is known to exhibit a lot of segmental motion, but its secondary structure is not wholly random coil; about one third of the polypeptide chain is ordered and the likely locations of these regions are discussed.
References
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Journal ArticleDOI

The determination of amino-acids with ninhydrin

TL;DR: A systematic review of the ninhydrin colour test for amino-acids is given in this article, with a note on its use in the identification of protein hydrolysates.
Journal ArticleDOI

A model for the myosin molecule

TL;DR: A model for the myosin molecule is proposed,based on three equal weight polypeptide chains in the form of a three-stranded α rope, based on X-ray diffraction, light scattering and optical rotatory data.
Book ChapterDOI

Optical rotation and the conformation of polypeptides and proteins.

TL;DR: An extension of the spectral range of measurement toward optically active absorption bands in the far ultraviolet is expected to yield new information about the rotatory power of the peptide bond and thus enhance the interaction of theory and observation that has already proved fruitful.