Results 321 to 330 of about 35,966 (338)
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Journal of Dairy Research, 1979
SUMMARYHuman β-casein occurs in multiphosphorylated forms having the same amino acid composition but with 0–5 phosphate groups/molecule. Sequence analysis was used to determine whether each of the phosphorylated forms is a mixture of species having a certain number of phosphate groups randomly distributed or whether each form contains phosphate groups ...
M L Groves, R Greenberg
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SUMMARYHuman β-casein occurs in multiphosphorylated forms having the same amino acid composition but with 0–5 phosphate groups/molecule. Sequence analysis was used to determine whether each of the phosphorylated forms is a mixture of species having a certain number of phosphate groups randomly distributed or whether each form contains phosphate groups ...
M L Groves, R Greenberg
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Casein micelle structure: location of κ-casein
Journal of Dairy Research, 1972SummaryThe effect of heat treatment on the rennet coagulation times (RCTs) of various casein–whey protein systems, the effect of pre-renneting centrifugal serum on the RCT of casein subsequently mixed with such serum, the influence of repeated centrifugation and resuspension at constant protein level on the RCT of such suspensions, and the rate and ...
Patrick A. Morrissey, Patrick F. Fox
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Structure of casein micelles II. ? s1-casein
Colloid & Polymer Science, 1987Following the earlier study of theβ- andϰ-casein micelle structure, we will now report results from theαs1-casein. Static and dynamic light scattering measurements were performed in a concentration range from 0.5 to 6.0 mg/ml atT=35 °C. A constant apparent molecular weight of 3.4×106 daltons was found over the whole range.
R. Niki +2 more
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Food Science and Technology International, 2006
Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation ...
Reyes Barberá +5 more
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Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation ...
Reyes Barberá +5 more
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Casein Micelles and Micelles of ϰ- and β-Casein
1982The tendency of proteins to associate in aqueous solution is well known. Most proteins form oligomers or undergo a series of consecutive association steps. A limited number, however, among which are ϰ- and β-casein, exhibit soaplike micellization.
T. A. J. Payens, H. J. Vreeman
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Journal of the Chemical Society, Faraday Transactions, 1997
The theoretical adsorption behaviour of the milk proteins, α s1 - and β-casein, has been studied using a self-consistent-field (SCF) model. Previously published results for β-casein on the effects of ionic strength and pH on protein conformation are compared with those for α s1 -casein. We find a lower adsorbed amount for α s1 -casein,
Dickinson, E. +3 more
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The theoretical adsorption behaviour of the milk proteins, α s1 - and β-casein, has been studied using a self-consistent-field (SCF) model. Previously published results for β-casein on the effects of ionic strength and pH on protein conformation are compared with those for α s1 -casein. We find a lower adsorbed amount for α s1 -casein,
Dickinson, E. +3 more
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Casein. VI.—determination of sialic acid in casein
Journal of the Science of Food and Agriculture, 1964AbstractSialic acid isolated from submaxillary gland and also from casein, and synthetic sialic acid have been used as standards in the determination of sialic acid in casein by the thio‐barbituric acid method. Consistently higher results for the apparent sialic acid content of casein were obtained with the synthetic sialic acid than with the sialic ...
Bruce E. Baker, Flora Y. Y. Huang
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κ-Casein and the Stabilization of Casein Micelles
Journal of the American Chemical Society, 1956Peter H. von Hippel, David F. Waugh
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