Literature DB >> 849471

Purification and some physicochemical properties of bovine kappa-casein.

H J Vreeman, P Both, J A Brinkhuis, C van der Spek.   

Abstract

1. A description is given of the fractionation of kappa-casein on DEAE-cellulose using a pH gradient. With this method an improved separation of the kappa-casein components with a higher negative charge is obtained. 2. It is shown that at least one of the kappa-casein fractions has a second phosphate ester group. The heterogeneity of kappa-casein therefore is not exclusively caused by a varying N-acetylneuraminic acid content. 3. Ultracentrifuge experiments and exclusion gel chromatography show that the purified kappa-casein fraction having the lowest electrophoretic mobility exhibits a monomer-polymer association equilibrium. The free energy of association per mol monomer in 0.2 M NaCl is approximately --36 kJ-mol-1.

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Year:  1977        PMID: 849471     DOI: 10.1016/0005-2795(77)90044-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Comparative Study of Action of Cell Wall Proteinases from Various Strains of Streptococcus cremoris on Bovine alpha(s1)-, beta-, and kappa-Casein.

Authors:  S Visser; F A Exterkate; C J Slangen; G J de Veer
Journal:  Appl Environ Microbiol       Date:  1986-11       Impact factor: 4.792

2.  Characterization of bovine kappa-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography.

Authors:  H J Vreeman; S Visser; C J Slangen; J A Van Riel
Journal:  Biochem J       Date:  1986-11-15       Impact factor: 3.857

  2 in total

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