Interaction between Hydroxyapatite and Collagen

2011 ◽  
Vol 412 ◽  
pp. 384-387 ◽  
Author(s):  
Zhao Long Huang ◽  
Gui Yang Liu ◽  
Ying He ◽  
Zhong Zhou Yi ◽  
Jun Ming Guo
Keyword(s):  
Calcium Phosphate ◽  
Calcium Ions ◽  
Ir Spectrum ◽  
Self Assembly ◽  
Calcium Ion ◽  
Cd Spectra ◽  
Layer Structures ◽  
Coordinate Bond ◽  
Strontium Ions ◽  
Strontium Ion

To study the interaction between hydroxyapatite (HAP) and collagen in bone, we researched the phenomenon of collagen biomineralization and self-assembly in viro by uv-vis spectra and circular dichroism (CD) spectra. The materials prepared by self-assembly collagen and collagen-HAP showed layer structures. And the product prepared by collagen-HAP had better and more compact appearance. The decrease of speed of collagen self-assembly was caused by calcium ion or strontium ion added. The trough of CD spectra moved down in calcium-containing solution and moved up when forming precipitation of calcium phosphate from the solution. It indicated that the effect of collagen self-assembly was caused by calcium ions, strontium ions etc. in the solution. The IR spectrum proved that a coordinate bond formed between calcium ion and amide groups on collagen.

The rennet hysteresis of heated milk

1969 ◽  
Vol 36 (3) ◽  
pp. 333-341 ◽  
Author(s):  
P. A. Morrissey
Keyword(s):  
Calcium Phosphate ◽  
Calcium Ions ◽  
Calcium Ion ◽  
Heating Process ◽  
Second Stage ◽  
Heated Milk ◽  
Rennet Coagulation ◽  
Micellar Casein ◽  
Induced Changes ◽  
Β Lactoglobulin

SummaryThe phenomenon of rennet hysteresis in heated milk is essentially due to reversible heat-induced changes of calcium phosphate equilibrium which affect the second or calcium ion stage of the rennet coagulation. The phenomenon is shown not only by heated milk but also by all heated caseinate systems provided they contain sufficient calcium to permit of coagulation with rennet and enough phosphate to ensure some degree of colloidal phosphate precipitation during the heating process; its occurrence does not require the presence of micellar casein or of β-lactoglobulin, or the initial presence of colloidal phosphate. Nevertheless, rennet hysteresis is greatly increased in these heated systems if β-lactoglobulin is present owing to the formation of a calcium caseinate/β-lactoglobulin complex which in its renneted condition is much less sensitive to calcium ions than is calcium para-caseinate. The resulting relative prolongation of the second stage of the rennet coagulation renders this phenomenon more apparent by increasing the proportion of the total time occupied by the hysteresis effect.

Calcium ion-assisted lipid tubule formation

2018 ◽  
Vol 2 (3) ◽  
pp. 603-608 ◽  
Author(s):  
Sandra Jones ◽  
An Huynh ◽  
Yuan Gao ◽  
Yan Yu
Keyword(s):  
Calcium Ions ◽  
Self Assembly ◽  
Calcium Ion ◽  
The Self ◽  
Tubule Formation

Calcium ions at mM concentrations promote the self-assembly of SOPC lipids into inter-connected hollow lipid tubes.

Study of Bio-Mineralization of BCP with Compensation of Calcium and Phosphate Ions

2009 ◽  
Vol 610-613 ◽  
pp. 1391-1394
Author(s):  
Hua De Zheng ◽  
Ying Jun Wang ◽  
Qiang Ma ◽  
Cheng Yun Ning ◽  
Xiao Feng Chen
Keyword(s):  
Free Energy ◽  
Calcium Phosphate ◽  
Calcium Ions ◽  
Biphasic Calcium Phosphate ◽  
Porous Ceramic ◽  
Apatite Layer ◽  
Apatite Formation ◽  
Phosphate Ions

In the present study, an Intelligent Multi-parameter Simulated Evaluation in vitro （IMSE system） was used to study the deposition properties of apatite formation on the surface of biphasic calcium phosphate porous ceramic (BCP) from static and dynamic r-SBF. Results showed that apatite formed on the surface of BCP from static and dynamic r-SBF differed between each other. In static r-SBF, ions were transferred by diffusion, which could not compensate the consuming of calcium ions, and mist apatite layer was formed on the surface of samples. But in the dynamic r-SBF, simulated fluid was adjusted precisely and flowed forcedly, the concentrations of ions were homogeneous; with the compensation of ions, calcium and phosphate were supersaturated, and the free energy of apatite formation was negative, bone-like apatite sheets were formed on the surface of samples.

scholarly journals THE EFFECT OF LACTIC ACID AND ARTIFICIAL SALIVA SOLUTION IMMERSION TO THE RELEASE OF CALCIUM IONS ON BIOACTIVE RESIN

2021 ◽  
Vol 6 (2) ◽  
pp. 190
Author(s):  
Dewi Puspitasari ◽  
Nurah Tajjalia ◽  
Diana Wibowo ◽  
Agung Satria Wardhana
Keyword(s):  
Lactic Acid ◽  
Acid Solution ◽  
Calcium Ions ◽  
Calcium Ion ◽  
Artificial Saliva ◽  
Distilled Water ◽  
Acid Condition ◽  
Ion Release ◽  
Lactic Acid Solution ◽  
Solution Increase

Background: Bioactive resin can release calcium ions when contact with solution media, even in acid condition. In the oral cavity, pH may change into acid condition due to the metabolic results of Streptococcus mutans. The bacteria metabolize carbohydrates into organic acids, one of which is lactic acid. Purpose: Analyze the effect of lactic acid solution and artificial saliva on the number of the release of calcium ions of bioactive resin. Methods: Forty-two specimens (diameter 15 mm x thickness 1 mm; n= 7/group fabricated with Activa™ Bioactive Restorative (Pulpdent). The specimens that meet the criteria were divided into 6 groups. The specimen was immersed for 1 and 7 days in the incubator at 37oC. The number of calcium ion release is measured using titration method. Results: Two Way Anova test and Post Hoc Bonferonni test showed there were significant differences among all group for lactic acid 1 day (4.040 ± 0.360) µg, artificial saliva 1 day (0.640 ± 0.338) µg, distilled water 1 day (1.040 ± 0.504) µg, lactic acid 7 days (5.400 ± 0.312), artificial saliva 7 days (1.640 ± 0.215) µg, distilled water 7 days (3.520± 0.356 µg). Conclusion: There was an influence of lactic acid and artificial saliva on the number of calcium ion releases of bioactive resin. Immersion of bioactive resin in the lactic acid solution increase the calcium ion releases and artificial saliva decrease the calcium ion release compared to distilled water. Keywords: artificial saliva, bioactive resin, calcium ion release, lactic acid

A fluoride selective water-soluble anion receptor based on a 1,2-phenylenediacetic acid and calcium ion dimer

2019 ◽  
Vol 43 (34) ◽  
pp. 13690-13695
Author(s):  
Dae Hyup Sohn ◽  
Nayeon Kim ◽  
Soonmin Jang ◽  
Jongmin Kang
Keyword(s):  
Calcium Ions ◽  
Calcium Ion ◽  
Water Soluble ◽  
Anion Receptor ◽  
Fluoride Ions

The dimeric receptor 1 from 1,2-phenylenediacetic acid and calcium ions recognized fluoride ions almost exclusively in 100% water.

HIGH AFFINITY CALCIUM BINDING TO DOMAINES OF PROTEIN C THAT ARE HOMOLOGUS TO THE EPIDERMAL GROWTH FACTOR

1987 ◽  
Author(s):  
A KÖhlin ◽  
J Stenflo
Keyword(s):  
Calcium Ions ◽  
Calcium Ion ◽  
Calcium Binding ◽  
Plasma Proteins ◽  
Metal Ion ◽  
Protein C ◽  
Protein S ◽  
Protein Z ◽  
High Affinity ◽  
Epidermal Growth

In addition to γ-carboxyglutamic acid (Gla)-dependent calcium binding all of the vitamin K-dependent plasma proteins, except prothrombin, have one or two high affinity calcium binding sites that do not require the Gla residues. A common denominator among these proteins (factors IX, X, protein C, protein Z and protein S) is that they have domaines that are homologus to the epidermal growth factor (EGF) precursor. In factors VII,IX,X, protein C and in protein Z the aminoterminal of two EGF homology regions contain one residue of β-hydroxyaspartic acid (Hya) whereas in protein S the aminoterminal EGF homology region contains Hya and the three following contain one β-hydroxyasparagine residue each.In an attempt to elucidate the role of the EGF homology regions in the Gla independent calcium binding we have isolated a tryptic fragment (residue 44-138) from the light chain of human protein C. The fragment was isolated using a monoclonal antibody that recognizes a calcium ion stabilized epitope that is expressed both in intact protein C and in protein C lacking the Gla domaine.The antibody bound the isolated EGF homology region in the presence of calcium ions but not in EDTA containing buffer. A calcium ion titration showed half maximal binding at approximately 200 μM Ca2+. The metal ion induced conformational change in the isolated fragment was also studied with affinity purified rabbit antibodies against Gla domainless protein C. Antibodies that bound in the presence of calcium ions and that could be eluted with EDTA recognized the metal ion induced conformational change in the isolated EGF homology domain. Our results suggest that one or both of the EGF homology regions are involved in the Gla-independent high affinity calcium binding in the vitamin K-dependent plasma proteins.

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