A Study on the Binding of Calcium Ions to<i>α</i><sub>s1</sub>-Casein

Ono, Tomotada; Kaminogawa, Shuichi; Odagiri, Satoshi; Yamauchi, Kunio

doi:10.1080/00021369.1976.10862299

Cited by 10 publications

(13 citation statements)

References 6 publications

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“…While calcium binds primarily to serine phosphate groups of the caseins, the major binding sites in -Lg are carboxylic acid groups. Also, calcium binds more strongly to phosphate than to carboxylic acid groups (16)(17)(18). The initial level of aggregation at the various calcium ion concentrations measured in this study thus agrees with the fact that caseinate binds more calcium, and with a higher affinity, than does -Lg.…”

Section: Discussionsupporting

confidence: 87%

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Agboola

Dalgleish

1996

LWT - Food Science and Technology

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Section: Discussionsupporting

confidence: 87%

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Agboola

Dalgleish

1996

LWT - Food Science and Technology

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“…Their binding ability depends on pH, ionie strength, temperature (PARKER and DALGLEISH, 1981) and the amount of phosphate in the solution (CREAMERand YAMASHITA,1976). The binding of more than 6.75 calcium ions on a (3-casein molecule causes its precipitation (PARKER and DALGLEISH,1981) : this result shows that binding to phosphoseryl and carboxylic residues is involved as demonstrated by ONO et al (1976) for OEsl-casein and by ONO et al (1980) for K-casein.…”

Section: Introductionmentioning

confidence: 91%

Effect of pH and ionic strength on the binding of bivalent cations to β-casein

Baumy

Brulé

1988

Lait

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SummaryThe binding capacity of (3-casein for Ca 2 +, Mg 2 +, Mn 2 +, Zn 2 +, Cu 2 +, Fe 2 + was studied at various pHs (from 8.00 to 5.00) and different ionie strengths (about 0, 0.05, 0.10).(3-casein can bind 7 bivalent cations atoms, at pH higher than 7.00 and low ionie strength, before precipitation occurs. For Ca 2 +, Mg +, Mn 2 +, Zn 2 + the binding ability decreases with pH or when ionie strength increases. For Cu 2 + and Fe 2 +, no effect of~H and ionie strength were detected. Affinity constants of (3-casein towards Ca 2 +, Mg +, Zn 2 + and Mn 2 + were investigated using SCATCHARD's plot at pH 6.60 and ionie strength = 0.10 ; it shows different kinds of binding sites (phosphoseryl, carboxylic) and different affinities for the cations corresponding to different kinds of links.Key words : (3-casein -Bivalent cations -Binding -pH -Ionie strength. Résumé Effet du pH et de la force ionique sur la fixation des cations bivalents par la caséine (3Une étude sur les capacités de fixation de la caséine (3 pour Ca 2 +, Mg 2 +, Mn 2 +, Zn 2 +, Cu 2 +, Fe 2 + a été réalisée à différents pH (de 8,00 à 5,00) et à différentes forces ioniques (0, 0,05, 0,10).A pH supérieur à 7,00 et à force ionique faible, la caséine~peut fixer jusqu'à 7 atomes de cations bivalents sans précipiter. Pour Ca 2 +, Mg 2 +, Mn + et Zn 2 + , ces capacités de fixation diminuent quand le pH chute ou quand la force ionique s'accroît. Ces deux caractéristiques du milieu n'ont pas d'influence sur la fixation du Cu 2 + et Fe 2 +. Les constantes d'affinité déterminées par la représentation de SCATC HARD de cette protéine vis-à-vis de Ca 2 +, Mg 2 +, Zn 2 + et Mn 2 + ont été déterminées à pH 6,60 et pour une force ionique de 0,10. Différents types de sites (phosphosériques et carboxyliques) ont été mis en évidence ; ils ont des affinités variables pour les cations et correspondent à différents types de liaison.

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“…8 ) The mean length increased with the increase in calcium concentration, which corresponded to the results obtained from ultracentrifugal analysis. 5 ) Calculations of probability distributions Since it is known that ()(sl-casein associates with K-casein in the absence of calcium, ()(slcasein has at least one binding site. Then, the following conditions are assumed to calculate the probability (P{i)) that i-mers of Unit are formed.…”

Section: Fig 3 Effect Of Calcium Concentration On the Meanmentioning

confidence: 99%

Polymerization of α_s1-Casein by Calcium Ions

Dosako

Kimura

Taneya

et al. 1980

Agricultural and Biological Chemistry

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O(,,-Casein was dissolved in 50 mM cacodylate-HCI-70 mM KCI buffer containing 0.02% of sodium azide (pH 7.1), and the size and shape of O(,,-caseins in the absence and presence of calcium ions were observed with the electron microscope. In the absence of calcium ions, most O(,,-caseins existed as spherical particles of which the smallest diameter was 5 -6 nm. The particles were polymerized into bent chains by adding 3 mM calcium. It seemed that the smallest particles were the polymerizing units. The mean length of O(,I-casein in the absence of calcium was 8.7 nm, and it increased as the calcium concentration increased. From these results, it was speculated that 0(,1-casein in the absence of calcium had one binding site and the calcium-induced confollnational changes produced a second binding site. The probability distributions were calculated with the above speculation, and compared with the frequency distributions obtained from electron micrographs. It was suggested from the comparisons that the second binding site produced in 0(,1-casein might be responsible for the calcium-induced aggregation.process.

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A Study on the Binding of Calcium Ions toα_s1-Casein

Cited by 10 publications

References 6 publications

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Effect of pH and ionic strength on the binding of bivalent cations to β-casein

Polymerization of α_s1-Casein by Calcium Ions

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A Study on the Binding of Calcium Ions toαs1-Casein

Cited by 10 publications

References 6 publications

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Effect of pH and ionic strength on the binding of bivalent cations to β-casein

Polymerization of αs1-Casein by Calcium Ions

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A Study on the Binding of Calcium Ions toα_s1-Casein

Polymerization of α_s1-Casein by Calcium Ions