Fabrication of ferritin-casein phosphopeptides-calcium shell-core composite as a novel calcium delivery strategy

2021 ◽  
Author(s):  
Lei Zhu ◽  
Lina Shi ◽  
Qiao-E Wang ◽  
Demei Meng ◽  
Zhongkai Zhou ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Binding Ability ◽  
Delivery Strategy ◽  
Casein Phosphopeptides ◽  
Bioactive Ingredients ◽  
Casein Phosphopeptide

Plant ferritin endows a natural cage-like nanospace for carrying bioactive ingredients. By taking advantage of the calcium binding ability of casein phosphopeptide (CPP) and the cage like conformation of plant...

Preparation of dextran–casein phosphopeptide conjugates, evaluation of its calcium binding capacity and digestion in vitro

2021 ◽  
pp. 129332
Author(s):  
Lan Jiang ◽  
Shuhong Li ◽  
Nan Wang ◽  
Shuang Zhao ◽  
Yue Chen ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Binding Capacity ◽  
Casein Phosphopeptide

scholarly journals Mechanism for Increase in Intracellular Concentration of Free Calcium in Fertilized Sea Urchin Egg

1974 ◽  
Vol 63 (3) ◽  
pp. 374-388 ◽  
Author(s):  
Masahisa Nakamura ◽  
Ikuo Yasumasu
Keyword(s):  
Dissociation Constant ◽  
Sea Urchin ◽  
Calcium Ion ◽  
Calcium Binding ◽  
Intracellular Concentration ◽  
Sodium Ion ◽  
Free Calcium ◽  
Binding Ability ◽  
Sea Urchin Egg ◽  
Fertilized Egg

Intracellular free calcium concentration in the sea urchin egg was calculated to increase from 0.1 mM in an unfertilized egg to 1 mM in a fertilized egg 10 min after fertilization, based on measurement of the dissociation constant between free calcium and sea urchin egg homogenate. The dissociation constant between free calcium (dialyzable calcium) and homogenate of sea urchin eggs was measured by means of dialysis equilibrium. The dissociation constant of the unfertilized egg was about 10–4 M and that of the fertilized egg was about 10–3 M in three species of sea urchin, Hemicentrotus pulcherrimus, Anthocidaris crassispina, and Pseudocentrotus depressus. An increase in the dissociation constant of the unfertilized egg homogenate was observed after the addition of calcium ion at a concentration above 0.3 mM, the dissociation constant becoming the same as that observed in the fertilized egg homogenate after the administration of CaCl2 at a concentration above 1 mM. Sodium ion also caused a decrease in the calcium-binding ability of the unfertilized egg homogenate. Therefore, penetration of calcium ion or sodium ion upon fertilization might induce an increase in the dissociation constant and then intracellular concentration of free calcium would increase at fertilization. Almost all calcium-binding ability of the egg homogenate was found in the microsomal fraction, and the substance which bound calcium was thought to be protein in nature, since trypsin could decrease the level of calcium-binding substance in the homogenate of the eggs.

Calcium-binding ability of soy protein hydrolysates

2007 ◽  
Vol 18 (9) ◽  
pp. 1115-1118 ◽  
Author(s):  
Xiao Lan Bao ◽  
Mei Song ◽  
Jing Zhang ◽  
Yang Chen ◽  
Shun Tang Guo
Keyword(s):  
Soy Protein ◽  
Calcium Binding ◽  
Protein Hydrolysates ◽  
Binding Ability ◽  
Soy Protein Hydrolysates

Calcium-45 binding by human prealbumin

1959 ◽  
Vol 14 (5) ◽  
pp. 859-860 ◽  
Author(s):  
Philip C. Johnson ◽  
William O Smith ◽  
Beulah Wulff
Keyword(s):  
Electrophoretic Mobility ◽  
Calcium Binding ◽  
Protein Separation ◽  
Gas Flow ◽  
Specific Activity ◽  
Tap Water ◽  
Paper Electrophoresis ◽  
Human Albumin ◽  
Binding Ability ◽  
Human Prealbumin

Calcium-45 binding by human albumin and prealbumin has been studied. Protein separation was performed by continuous paper electrophoresis. Calcium-45 was added to the fractions and the mixture incubated at 37℃ for 24 hours. Unbound calcium-45 was removed by dialysis against tap water for 16 hours, the pH of the fractions remained between 8.6–9.1 at all times. Aliquots of the fractions were then counted with a micromil gas flow counter. The greatest specific activity was found in several tubes preceding the albumin, i.e. with faster electrophoretic mobility than classical albumin. The calcium-binding ability of this fraction, which has been previously called ‘prealbumin,’ exceeded that of classical albumin by sixfold. Submitted on December 1, 1958

Calcium Accumulation and Calcium Binding by the Cell Membranes of Cardiomyocytes and Smooth Muscle of Aorta in Spontaneously Hypertensive Rats

1980 ◽  
Vol 59 (s6) ◽  
pp. 207s-209s ◽  
Author(s):  
S. N. Orlov ◽  
Yu. V. Postnov
Keyword(s):  
Smooth Muscle ◽  
Erythrocyte Membrane ◽  
Calcium Binding ◽  
Spontaneously Hypertensive Rats ◽  
Plasma Membranes ◽  
Hypertensive Rats ◽  
Binding Ability ◽  
Spontaneously Hypertensive ◽  
Aortic Smooth Muscle ◽  
Lower Ability

1. The ability of isolated membrane fractions of cardiomyocytes, aortic smooth muscle and erythrocytes from spontaneously hypertensive rats to bind calcium was investigated isotopically. 2. Plasma membranes of aortic smooth muscle and erythrocytes of spontaneously hypertensive rats possess a lower calcium-binding ability than preparations from normotensive controls. 3. Sarcoplasmic reticulum from the myocardium of spontaneously hypertensive rats had a lower ability to accumulate calcium. 4. Changes in the calcium-binding ability of the erythrocyte membrane of spontaneously hypertensive rats was related to the diminution of the amount of exchangeable calcium on the inner part of the membrane. The latter may be the cause of the increase of erythrocyte membrane permeability for sodium in spontaneously hypertensive rats and in patients with essential hypertension.

Preparation of Phytate-Removed Deamidated Soybean Globulins by Ion Exchangers and Characterization of Their Calcium-Binding Ability

2002 ◽  
Vol 50 (1) ◽  
pp. 172-176 ◽  
Author(s):  
Hitomi Kumagai ◽  
Shigeo Ishida ◽  
Atsushi Koizumi ◽  
Hidetoshi Sakurai ◽  
Hitoshi Kumagai
Keyword(s):  
Calcium Binding ◽  
Ion Exchangers ◽  
Binding Ability ◽  
Soybean Globulins

scholarly journals Antioxidant Properties of Casein Phosphopeptides (CPP) and Maillard-Type Conjugated Products

Antioxidants ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 648
Author(s):  
Huiying Zhang ◽  
Soichiro Nakamura ◽  
David D. Kitts
Keyword(s):  
Antioxidant Activity ◽  
Metal Ion ◽  
Fenton Reaction ◽  
Soybean Lecithin ◽  
Antioxidant Properties ◽  
Aqueous System ◽  
Binding Assays ◽  
Site Specific ◽  
Casein Phosphopeptides ◽  
Casein Phosphopeptide

A casein phosphopeptide (CPP) fraction derived from tryptic hydrolysis of bovine casein was evaluated for antioxidant activity. Conjugations or mixtures of CPP with polysaccharide, galactomannan (Gal), or xyloglucan (Xyl) were prepared to evaluate potential enhancement of CPP antioxidant activity. The effect of calcium was also investigated. The CPP preparation alone was effective at scavenging hydroxyl radicals and sequestering Fe2+ to protect against Fenton reaction-induced deoxyribose oxidation in non-site-specific (up 63.3% inhibition) and site-specific (up 32.1% inhibition) binding assays, respectively. CPP also effectively quenched 2,2’-azinobis-3-ethylbenzothiazoline-6-sulfonic acid radicals (ABTS•+) to an extent of 67.6% scavenging in an aqueous system. In a soybean lecithin liposome system, CPP exhibited effective protection against peroxyl radical-induced liposomal peroxidation (38.3% of control in terms of rate of propagation). Conjugating CPP with Gal or Xyl polysaccharides using Maillard reaction conditions significantly reduced activity in the Fenton reaction-deoxyribose assays, while exhibiting no effect on the antioxidant activity of native CPP in both the ABTS and liposome assays, respectively. These results represent comparative antioxidant capacity of the native CPP and associated conjugates in phases that varied in relative hydrophilic and hydrophobic character. We conclude that CPP has the potential to act as both a primary and secondary antioxidant by displaying transition metal ion sequestering activity and free radical quenching activity. Improvements in antioxidant activity of CPP by Maillard-type conjugation with Xyl or Gal were relatively small and model-specific.

Calcium Binding Ability of Recombinant Buffalo Regucalcin: A Study Using Circular Dichroism Spectroscopy

2017 ◽  
Vol 36 (2) ◽  
pp. 108-111 ◽  
Author(s):  
P. Harikrishna ◽  
Jobin Thomas ◽  
A. M. Shende ◽  
S. K. Bhure
Keyword(s):  
Circular Dichroism ◽  
Calcium Binding ◽  
Circular Dichroism Spectroscopy ◽  
Binding Ability ◽  
Circular Dichroïsm

scholarly journals The Nucleolar Channel System of Human Endometrium Is Related to Endoplasmic Reticulum and R-Rings

2007 ◽  
Vol 18 (6) ◽  
pp. 2296-2304 ◽  
Author(s):  
Nupur Kittur ◽  
Gregory Zapantis ◽  
Mira Aubuchon ◽  
Nanette Santoro ◽  
David P. Bazett-Jones ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Binding ◽  
Ring Formation ◽  
Binding Ability ◽  
Channel System ◽  
Culture Cells ◽  
Human Fertility ◽  
Repeat Domain ◽  
And Function

The nucleolar channel system (NCS) is a well-established ultrastructural hallmark of the postovulation endometrium. Its transient presence has been associated with human fertility. Nevertheless, the biogenesis, composition, and function of these intranuclear membrane cisternae are unknown. Membrane systems with a striking ultrastructural resemblance to the NCS, termed R-rings, are induced in nuclei of tissue culture cells by overexpression of the central repeat domain of the nucleolar protein Nopp140. Here we provide a first molecular characterization of the NCS and compare the biogenesis of these two enigmatic organelles. Like the R-rings, the NCS consists of endoplasmic reticulum harboring the marker glucose-6-phosphatase. R-ring formation initiates at the nuclear envelope, apparently by a calcium-mediated Nopp140-membrane interaction, as supported by the calcium-binding ability of Nopp140, the inhibition of R-ring formation by calcium chelators, and the concentration of Nopp140 and complexed calcium in R-rings. Although biogenesis of the NCS may initiate similarly, the reduced presence of complexed calcium and Nopp140 suggests the involvement of additional factors.

scholarly journals Effect of Bound Phosphate on the Calcium-binding Ability and Calcium-dependent Precipitability of Human β-Casein

1989 ◽  
Vol 53 (4) ◽  
pp. 1037-1041
Author(s):  
Norihiro Azuma ◽  
Masayuki Aizawa ◽  
Kunio Yamauchi
Keyword(s):  
Calcium Binding ◽  
Binding Ability ◽  
Calcium Dependent
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