Biochemical and histochemical characteristics of proteins homologous to calf lens membrane proteins with high calcium-binding capacity

1985 ◽  
Vol 159 (2) ◽  
pp. 519-530 ◽  
Author(s):  
A.J.M. Van den Eijnden-van Raaij ◽  
A.L.M. De Leeuw ◽  
H.J. Winkens ◽  
J.F.J. Kruisselbrink-Borgonjen ◽  
R.M. Broekhuyse
Keyword(s):  
Membrane Proteins ◽  
Calcium Binding ◽  
Binding Capacity ◽  
High Calcium

Changes in the secondary structures and zeta potential of soybean peptide and its calcium complexes in cell membrane medium

2021 ◽  
Author(s):  
He Liu ◽  
Ying Lv ◽  
Jingting Xu ◽  
Chen Chen ◽  
Shuntang Guo
Keyword(s):  
Enzymatic Hydrolysis ◽  
Cell Membrane ◽  
Zeta Potential ◽  
Calcium Binding ◽  
Binding Capacity ◽  
Secondary Structures ◽  
High Calcium ◽  
Calcium Complexes

In this study, soybean peptides (10-30kDa) with high calcium binding capacity were prepared by enzymatic hydrolysis and ultrafiltration. The results of cell experiments showed that the peptide could transport calcium...

scholarly journals Elucidating the Calcium-Binding Site, Absorption Activities, and Thermal Stability of Egg White Peptide–Calcium Chelate

Foods ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 2565
Author(s):  
Zhijie Bao ◽  
Penglin Zhang ◽  
Na Sun ◽  
Songyi Lin
Keyword(s):  
Calcium Binding ◽  
Calcium Absorption ◽  
Binding Capacity ◽  
Egg White ◽  
Absorption Capacity ◽  
Spherical Particles ◽  
Calcium Binding Site ◽  
Peptide Bonds ◽  
High Calcium ◽  
Α Helix

With the current study, we aimed to determine the characteristics and calcium absorption capacity of egg white peptide–calcium complex (EWP-Ca) and determine the effect of sterilization on EWP-Ca to study the possibility of EWP-Ca as a new potential calcium supplement. The results of SEM and EDS showed a high calcium chelating ability between EWP and calcium, and the structure of EWP-Ca was clustered spherical particles due its combination with calcium. The FTIR and Raman spectrum results showed that EWP could chelate with calcium by carboxyl, phosphate, and amino groups, and peptide bonds may also participate in peptide–calcium binding. Moreover, the calcium absorption of EWP-Ca measured by the intestinal everted sac model in rats was 32.38 ± 6.83 μg/mL, significantly higher than the sample with CaCl2, and the mixture of EWP and Ca (p < 0.05) revealed appropriate calcium absorption capacity. The fluorescence spectra and CD spectra showed that sterilization caused a decrease in the content of α-helix and β-sheet and a significant increase in β-turn (p < 0.05). Sterilization changed the EWP-Ca structure and decreased its stability; the calcium-binding capacity of EWP-Ca after sterilization was decreased to 41.19% (p < 0.05). Overall, these findings showed that EWP could bind with calcium, form a peptide–calcium chelate, and serve as novel carriers for calcium supplements.

Anti-osteoporosis effect and purification of peptides with high calcium-binding capacity from walnut protein hydrolysate

2021 ◽  
Author(s):  
Sun Xiaodong ◽  
Ruan Shiyan ◽  
Yongliang Zhuang ◽  
Sun Liping
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Calcium Binding ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Degree Of Hydrolysis ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
High Calcium ◽  
Relative Molecular Weight

Walnut protein hydrolysate (WPH) was prepared via simulated gastrointestinal digestion. The degree of hydrolysis (DH), amino acid composition, and relative molecular weight distribution of WPH were analyzed. Results showed that...

The Relationship between the Hydrolysis Degree and Calcium-Binding Capacity of Whey Protein by Enzymatic Hydrolysis

2014 ◽  
Vol 541-542 ◽  
pp. 214-219 ◽  
Author(s):  
Li Na Zhao ◽  
Shao Yun Wang ◽  
Shun Li Huang ◽  
Yi Fan Huang
Keyword(s):  
Enzymatic Hydrolysis ◽  
Whey Protein ◽  
Calcium Binding ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Optimum Process ◽  
Hydrolysis Degree ◽  
High Calcium ◽  
Whey Protein Hydrolysate ◽  
The Relationship

To study the relationship between the hydrolysis degree and calcium-binding capacity of whey protein by enzymatic hydrolysis, the response surface method was firstly used to investigate optimized the hydrolysis conditions of whey protein with protamex and flavorzyme. The optimum process parameters for the whey protein hydrolysis were as follows: Whey protein concentration was 5.0% (w/v), the ratio of protease to whey protein was 4.0% (w/w), the mass ratios of protamex to flavorzyme (w/w) was 2:1, and the reaction temperature was 49 °C. The hydrolysate obtained after the hydrolysis of 7 h, with a hydrolysis degree of 25.92%, possessed the highest Ca-binding capacity of 27.92%. Finally, the relationship between the hydrolysis degree and calcium-binding capacity was established and whey protein hydrolysate with high calcium-binding capacity was prepared, which can provide basic theories for the following optimization of chelation of whey protein hydrolysate with calcium.

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

Fibrinogen Bern I: A Hereditary Fibrinogen Variant With Defective Conformational Stabilization By Calcium Ions

1981 ◽  
Author(s):  
C Rupp ◽  
C Kuyas ◽  
A Häberli ◽  
M Furlan ◽  
E A Beck
Keyword(s):  
Calcium Ions ◽  
Gel Electrophoresis ◽  
Calcium Binding ◽  
Negative Charge ◽  
Fibrinopeptide A ◽  
Isoelectric Focussing ◽  
High Calcium ◽  
Two Generations ◽  
Polypeptide Chains ◽  
Conformational Stabilization

Inherited hypodysfibrinogenemia (fibrinogen Bern I) was found in four members (two generations) of a family with no haemorrhagic or thrombotic history. Fibrin aggregation curves (350 nm, 37°C) with patient plasma or purified fibrinogen Bern I, after addition of thrombin, were normal at high calcium concentrations (5mM) but delayed at lower calcium concentrations (≤0.lmM). The release of fibrinopeptide A was normal. Whereas the polypeptide chains of fibrinogen Bern I were indistinguishable from normal fibrinogen by SDS-gel-electrophoresis, an abnormal γ-chain with a decreased negative charge was found by isoelectric focussing.Plasmic degradation o| normal fibrinogen, in the presence of calcium (≥ImM), results in only one terminal D fragment which is stabilized by calcium against further degradation of γ-chains. In contrast, degradation of fibrinogen Bern I, under the same conditions, yielded at least two additional smaller D fragments. In conclusion, fibrinogen Bern I is characterized by defective calcium binding in the D domain of the γ-chain.

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