scholarly journals Identification and characterization of a calcium-binding protein in the mouse chorioallantoic placenta

1986 ◽  
Vol 233 (1) ◽  
pp. 41-49 ◽  
Author(s):  
R S Tuan ◽  
S T Cavanaugh
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Calcium Binding Protein ◽  
Chorionic Villi ◽  
Chorioallantoic Placenta ◽  
Identification And Characterization

Mouse chorioallantoic placenta contains a specific calcium-binding protein (MCaBP). A procedure involving gel filtration and ion-exchange chromatography was developed to purify the MCaBP. The MCaBP activity increased as a function of embryonic gestation and was highly specific for Ca2+. The MCaBP is a monomeric protein of Mr 57000, with pI 4.7. Specific antibodies were prepared against the MCaBP and were used to localize the MCaBP to syncytiotrophoblasts of the chorionic villi of mouse chorioallantoic placenta. These properties suggest that the MCaBP may be involved in transplacental calcium transport.

Preparation and Characterization of NH2-Terminal Fibrinogen Bβ Fragments from N-DSK of Human Fibrinogen

1984 ◽  
Vol 51 (01) ◽  
pp. 016-021 ◽  
Author(s):  
S Birken ◽  
G Agosto ◽  
B Lahiri ◽  
R Canfield
Keyword(s):  
High Performance ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Reverse Phase ◽  
Human Fibrinogen ◽  
Human Volunteers ◽  
Cnbr Cleavage ◽  
Two Peaks

SummaryIn order to investigate the early release of NH2-terminal plasmic fragments from the Bβ chain of fibrinogen, substantial quantities of Bβ 1-42 and Bβ 1-21 are required as immunogens, as radioimmunoassay standards and for infusion into human volunteers to determine the half-lives of these peptides. Towards this end methods that employ selective proteolytic cleavage of these fragments from fibrinogen have been developed. Both the N-DSK fragment, produced by CNBr cleavage of fibrinogen, and Bβ 1-118 were employed as substrates for plasmin with the finding of higher yields from N-DSK. Bβ 1-42 and Bβ 1-21 were purified by gel filtration and ion-exchange chromatography on SP-Sephadex using volatile buffers. When the purified preparation of Bβ 1-42 was chromatographed on reverse-phase high performance liquid chromatography, two peaks of identical amino acid composition were separated, presumably due either to pyroglutamate or to amide differences.

Cloning and characterization of an immunoreactive gene encoding a calcium-binding protein from Naegleria fowleri

2004 ◽  
Vol 137 (1) ◽  
pp. 169-173 ◽  
Author(s):  
Seok-Ryoul Jeong ◽  
Myung-Soo Cho ◽  
Sun Park ◽  
Kyongmin Hwang Kim ◽  
Kyoung-Ju Song ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Naegleria Fowleri ◽  
Gene Encoding ◽  
Nægleria Fowleri

Radioimmunoassay Studies of Intestinal Calcium-binding Protein in the Pig. II. The Distribution of Intestinal CaBP in Pig Tissues

1975 ◽  
Vol 53 (6) ◽  
pp. 1135-1140 ◽  
Author(s):  
B. M. Arnold ◽  
M. Kuttner ◽  
D. M. Willis ◽  
A. J. W. Hitchman ◽  
J. E. Harrison ◽  
...  
Keyword(s):  
Small Intestine ◽  
Calcium Binding ◽  
Binding Protein ◽  
Gel Filtration ◽  
Protein S ◽  
Binding Activity ◽  
Calcium Binding Protein ◽  
Distal Small Intestine ◽  
Specific Radioimmunoassay ◽  
Kidney Liver

Using a specific radioimmunoassay for porcine intestinal calcium-binding protein (CaBP), we have measured the concentration of CaBP in the various tissues and organs of normal pigs. Intestinal CaBP was present in highest concentration in the upper small intestine, with lower concentrations in the distal small intestine. Intestinal CaBP was also found, in lower concentrations, in kidney, liver, thyroid, pancreas, and blood. In all other tissues, including parathyroid, bone, skeletal muscle, and brain, CaBP immunoreactivity was undetectable or less than in blood. The elution profile of calcium-binding activity and immunoreactivity from gel filtration analysis of kidney and parathyroid extracts suggest that the calcium-binding protein in the parathyroid gland, and the major calcium-binding protein(s) in the kidney, are chemically and immunochemically different from intestinal CaBP.

scholarly journals Isolation and characterization of grancalcin, a novel 28 kDa EF-hand calcium-binding protein from human neutrophils

1992 ◽  
Vol 286 (2) ◽  
pp. 549-554 ◽  
Author(s):  
C G Teahan ◽  
N F Totty ◽  
A W Segal
Keyword(s):  
Sequence Analysis ◽  
Calcium Binding ◽  
Binding Protein ◽  
Sequence Similarity ◽  
Gel Filtration ◽  
Calcium Binding Protein ◽  
Peptide Sequence ◽  
Human Neutrophils ◽  
Isolation And Characterization ◽  
Ef Hand

A novel 28 kDa protein, which we have named ‘grancalcin’, has been identified in human neutrophils. The protein was isolated from the cytosol and found to be a homodimer, with an apparent molecular mass of 55 kDa on gel filtration. Polyclonal antibodies were raised to the native protein. N-Terminal sequence analysis and tryptic-peptide sequence analysis was performed. The protein exhibits sequence similarity to sorcin, a 24 kDa calcium-binding protein over-expressed in certain multi-drug-resistant cell lines. It appears to be a member of the EF-hand family of calcium-binding proteins. The association of a high proportion of this protein with the membranes and granules in the presence of physiological concentrations of calcium may indicate a role in granule-membrane fusion and degranulation.

Sign in / Sign up

Export Citation Format

Share Document