Calcium Binding Peptides from α-Lactalbumin:  Implications for Protein Folding and Stability†

Biochemistry ◽  
1997 ◽  
Vol 36 (15) ◽  
pp. 4607-4615 ◽  
Author(s):  
Brian Kuhlman ◽  
Judith A. Boice ◽  
Wen-Jin Wu ◽  
Robert Fairman ◽  
Daniel P. Raleigh
Keyword(s):  
Protein Folding ◽  
Calcium Binding ◽  
Binding Peptides

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 peptides from the gills, gut and kidneys of the freshwater eel (Anguilla anguilla)

1978 ◽  
Vol 536 (2) ◽  
pp. 429-432 ◽  
Author(s):  
Peter R. Hearn ◽  
Stephen Tomlinson ◽  
Homa Mellersh ◽  
Christopher J. Kenyon ◽  
Christopher J. Preston ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Anguilla Anguilla ◽  
High Affinity ◽  
Freshwater Eel ◽  
Binding Peptides

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

scholarly journals Role of Calcium in Protein Folding and Function of Tva, the Receptor of Subgroup A Avian Sarcoma and Leukosis Virus

2001 ◽  
Vol 75 (5) ◽  
pp. 2051-2058 ◽  
Author(s):  
Qing-Yin Wang ◽  
Klavs Dolmer ◽  
Wen Huang ◽  
Peter G. W. Gettins ◽  
Lijun Rong
Keyword(s):  
Protein Folding ◽  
Calcium Binding ◽  
Titration Calorimetry ◽  
Viral Receptor ◽  
Calcium Affinity ◽  
Binding Residues ◽  
And Function ◽  
Avian Sarcoma

ABSTRACT Tva is the cellular receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A). The viral receptor function of Tva is determined by a 40-residue cysteine-rich motif called the LDL-A module. In this study, we expressed and purified the wild-type (wt) Tva LDL-A module as well as several mutants and examined their in vitro folding properties. We found that, as for other LDL-A modules, correct folding and structure of the Tva LDL-A module is Ca2+ dependent. When calcium was present during in vitro protein folding, the wt module was eluted as a single peak by reverse-phase high-pressure liquid chromatography. Furthermore, two-dimensional nuclear magnetic resonance (NMR) spectroscopy gave well-dispersed spectra in the presence of calcium. In contrast, the same protein folded in vitro in the absence of calcium was eluted as multiple broad peaks and gave a poorly dispersed NMR spectrum in the presence of calcium. The calcium affinity (Kd ) of the Tva LDL-A module, determined by isothermal titration calorimetry, is approximately 40 μM. Characterization of several Tva mutants provided further evidence that calcium is important in protein folding and function of Tva. Mutations of the Ca2+-binding residues (D46A and E47A) completely abrogated the Ca2+-binding ability of Tva, and the proteins were not correctly folded. Interestingly, mutations of two non-calcium-binding residues (W48A and L34A) also exerted adverse effect on Ca2+-dependent folding, albeit to a much less extent. Our results provide new insights regarding the structure and function of Tva in ASLV-A entry.

scholarly journals Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding

2001 ◽  
Vol 357 (1) ◽  
pp. 83 ◽  
Author(s):  
Barbara KRAMER ◽  
David M. FERRARI ◽  
Peter KLAPPA ◽  
Nicole PÖHLMANN ◽  
Hans-Dieter SÖLING
Keyword(s):  
Protein Folding ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Functional Roles

ChemInform Abstract: Synthetic Calcium-Binding Peptides

ChemInform ◽  
2010 ◽  
Vol 33 (48) ◽  
pp. no-no
Author(s):  
Gary S. Shaw
Keyword(s):  
Calcium Binding ◽  
Binding Peptides
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