scholarly journals 1K1400 Analysis of the interaction between synthetic calcium binding peptides and a metal ion by infrared spectroscopy

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S63
Author(s):  
M. Nara ◽  
H. Morii ◽  
F. Yumoto ◽  
H. Kagi ◽  
M. Tanokura
Keyword(s):  
Infrared Spectroscopy ◽  
Calcium Binding ◽  
Metal Ion ◽  
Binding Peptides

Frontiers in the infrared spectroscopy of gas phase metal ion complexes

2005 ◽  
Vol 29 (12) ◽  
pp. 1495 ◽  
Author(s):  
Nicholas R. Walker ◽  
Richard S. Walters ◽  
Michael A. Duncan
Keyword(s):  
Infrared Spectroscopy ◽  
Gas Phase ◽  
Metal Ion ◽  
Metal Ion Complexes

Nuclear proteins of the bovine esophageal epithelium. I. Monoclonal antibody W2 specifically reacts with condensed nuclei of differentiated superficial cells

1993 ◽  
Vol 104 (2) ◽  
pp. 237-247 ◽  
Author(s):  
T.K. Tang ◽  
T.M. Hong ◽  
C.Y. Lin ◽  
M.L. Lai ◽  
C.H. Liu ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Metal Ion ◽  
Gradient Centrifugation ◽  
Basal Layer ◽  
Small Cells ◽  
Target Antigen ◽  
Esophageal Epithelium ◽  
Nuclear Condensation ◽  
Calcium Binding Site

Cells from three layers of the bovine esophageal epithelium, representing different stages of differentiation, were dissociated and separated by Percoll gradient centrifugation into fractions of small, medium and large sizes. A majority of the large cells possessed condensed nuclei, a characteristic feature of terminal differentiation of the superficial epithelium. The small cells resembled the proliferate cells of the basal layer. In vitro culture of the esophageal epithelial cells resulted in proliferation of the small cells, colony formation, and, in some cases, differentiation into cells with condensed nuclei. Nuclei, or nuclear subfractions derived from cells of the different layers, were used as immunogens for the generation of hybridomas secreting monoclonal antibodies that bound specifically to different regions of the esophageal tissue. One such antibody, designated W2, labeled the condensed nuclei from the superficial layer of stratified esophageal and corneal epithelia in situ, as well as the large cells from esophageal culture in vitro. Thus, the expression of the W2 antigen may be associated with the process of nuclear condensation during epithelial differentiation. Immunoisolation of the target antigen of W2 from extracts of large cells of the bovine esophagus yielded a band of M(r) approximately 33,000 on nonreducing polyacrylamide gels. This band dissociated into two polypeptides, of M(r) approximately 22,000 and approximately 11,000, upon treatment with dithiothreitol. Amino acid sequence analysis of the larger polypeptide showed extensive homology to a group of small calcium-binding proteins, including two helix-turn-helix motifs designated as the EF-hand, characteristic of the configuration of the metal-ion coordinating ligands of the calcium-binding site. Similarly, the sequence at the amino terminus of the polypeptide of approximately 11,000 indicated that it was the light chain counterpart of the same calcium-binding protein complex.

scholarly journals Functional Calcium Binding Peptides from Pacific Cod (Gadus macrocephalus) Bone: Calcium Bioavailability Enhancing Activity and Anti-Osteoporosis Effects in the Ovariectomy-Induced Osteoporosis Rat Model

Nutrients ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 1325 ◽  
Author(s):  
Kai Zhang ◽  
Bafang Li ◽  
Qianru Chen ◽  
Zhaohui Zhang ◽  
Xue Zhao ◽  
...  
Keyword(s):  
Serum Calcium ◽  
Rat Model ◽  
Calcium Binding ◽  
Calcium Absorption ◽  
Intestinal Calcium Absorption ◽  
Pacific Cod ◽  
Pacific Cod Gadus Macrocephalus ◽  
Calcium Bioavailability ◽  
Gadus Macrocephalus ◽  
Binding Peptides

Calcium binding peptides from Pacific cod (Gadus macrocephalus) bone have attracted attention due to their potential effects on bone health. In this study, calcium binding peptides (CBP) were prepared from Pacific cod bone by trypsin and neutral protease. Ultraviolet spectra, circular dichroism (CD), and Fourier transform infrared spectroscopy (FTIR) revealed that carboxyl and amino groups in CBP could bind to Ca2+, and form the peptide-calcium complex (CBP-Ca). Single-pass intestinal perfusion (SPIP) experiments indicated that the intestinal calcium absorption was significantly enhanced (p < 0.01) in CBP-Ca treated Wistar rats. The anti-osteoporosis activity of CBP-Ca was investigated in the ovariectomized (OVX) Wistar rat model. The administration of CBP-Ca significantly (p < 0.01) improved the calcium bioavailability, trabecular bone structure, bone biomechanical properties, bone mineral density, and bone mineralization degree. CBP-Ca notably (p < 0.01) increased serum calcium, however, it remarkably (p < 0.01) reduced the levels of osteocalcin (OCN), bone alkaline phosphatase (BALP), tartrate-resistant acid phosphatase isoform 5b (TRAP5b), and C-telopeptide of type I collagen (CTX-1) in serum. Results suggested that the cod bone derived CBP could bind with calcium, improve the intestinal calcium absorption, calcium bioavailability, and serum calcium, then reduce the bone turnover rate, and thus ameliorate osteoporosis.

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.

Locating the Metal Ion in Calcium-Binding Proteins by Using Cerium(III) as a Probe

ChemBioChem ◽  
2001 ◽  
Vol 2 (7-8) ◽  
pp. 550-558 ◽  
Author(s):  
Ivano Bertini ◽  
Yong-Min Lee ◽  
Claudio Luchinat ◽  
Mario Piccioli ◽  
Luisa Poggi
Keyword(s):  
Calcium Binding ◽  
Metal Ion ◽  
Binding Proteins ◽  
Calcium Binding Proteins

Metal Ion-Driven Assembly of Two New Coordination Polymers Constructed by Asymmetric Tricarboxylate and Imidazole-Containing Ligands: Syntheses, Crystal Structures, and Luminescent Properties

2015 ◽  
Vol 68 (1) ◽  
pp. 121 ◽  
Author(s):  
Wenlong Liu ◽  
Xueying Wang ◽  
Mengqiang Wu ◽  
Bing Wang
Keyword(s):  
Infrared Spectroscopy ◽  
Coordination Polymers ◽  
Metal Ion ◽  
Three Dimensional ◽  
Luminescent Properties ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
Hydrothermal Conditions ◽  
X Ray ◽  
Dimethyl Benzene

Two new coordination polymers, namely, {[Cd3(bpt)2(bimb)2]·2(H2O)}n (1) and [Zn3(bpt)2(bimb)2]n (2) (bpt = biphenyl-3,4′,5-tricarboxylate, bimb = 1,4-bis(1-imidazol-yl)-2,5-dimethyl benzene), have been obtained under hydrothermal conditions. Their structures have been determined by single-crystal X-ray diffraction analysis and further characterised by elemental analysis and infrared spectroscopy. Complex 1 exhibits a trinodal (4,4,4)-connected topology with Schläfli symbol of (4.62.83)4.(64.82). Complex 2 is also a three-dimensional structure and displays a (3,4,6)-connected topology with Schläfli symbol of (4.62)2.(42.66.85.102).(64.82). It is shown that the asymmetrically tricarboxylate can bear diverse structures regulated by metal ions. The photoluminescence behaviours of compounds 1 and 2 were also discussed.

Sign in / Sign up

Export Citation Format

Share Document