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.

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.

Differential expression of the EF-hand calcium-binding protein calsensin in the central nervous system of hirudinid leeches

1996 ◽  
Vol 286 (3) ◽  
pp. 357-364 ◽  
Author(s):  
Mark Veldman ◽  
Yueqiao Huang ◽  
John Jellies ◽  
Kristen M. Johansen ◽  
Jørgen Johansen
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Differential Expression ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Ef Hand ◽  
The Central Nervous System

NMR Derived Solution Structure of an EF-Hand Calcium-Binding Protein fromEntamoeba Histolytica†

Biochemistry ◽  
2001 ◽  
Vol 40 (48) ◽  
pp. 14392-14403 ◽  
Author(s):  
H. S. Atreya ◽  
S. C. Sahu ◽  
A. Bhattacharya ◽  
Girjesh Govil
Keyword(s):  
Calcium Binding ◽  
Solution Structure ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Ef Hand
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