scholarly journals Calcium-binding protein in the duodenal mucosa of uremic patients and normal subjects

1975 ◽  
Vol 8 (2) ◽  
pp. 110-118 ◽  
Author(s):  
Peter Piazolo ◽  
Jürgen Hotz ◽  
Klaus Helmke ◽  
Hans-Eduard Franz ◽  
Mark Schleyer
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Normal Subjects ◽  
Duodenal Mucosa ◽  
Calcium Binding Protein ◽  
Uremic Patients

scholarly journals Messenger ribonucleic acids from pig intestinal mucosa direct synthesis of calcium-binding protein in a cell-free translation system

1980 ◽  
Vol 185 (3) ◽  
pp. 601-607 ◽  
Author(s):  
H Mellersh ◽  
S Tomlinson ◽  
A Pollock
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Direct Synthesis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Duodenal Mucosa ◽  
Exchange Chromatography ◽  
Calcium Binding Protein ◽  
Translation System ◽  
Free System

mRNA from pig duodenal mucosa directs synthesis, in a wheat-germ cell-free system, of two products precipitated by antiserum to pure calcium-binding protein. One of these products has a higher molecular weight than authentic calcium-binding protein, but, like the authentic protein, is heat-stable. The other protein co-migrates with pure calcium-binding protein on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, is stable on heating to 70 degrees C for 15 min and alters its elution position on ion-exchange chromatography depending on whether Ca2+ is present in or absent from the elution buffer. The synthesized protein has these properties in common with authentic calcium-binding protein.

Calcium Binding Proteins in the Duodenal Mucosa of the Chick, Rat, Pig, and Human

1972 ◽  
Vol 50 (7) ◽  
pp. 758-765 ◽  
Author(s):  
A. J. W. Hitchman ◽  
Joan E. Harrison
Keyword(s):  
Molecular Weight ◽  
Vitamin D ◽  
Calcium Ions ◽  
Calcium Binding ◽  
Binding Protein ◽  
Gel Filtration ◽  
Duodenal Mucosa ◽  
Calcium Binding Proteins ◽  
Calcium Binding Protein ◽  
Electrophoretic Mobilities

A calcium binding protein has been demonstrated in human duodenal mucosa which we believe to be human vitamin D dependent CaBP. Sephadex gel filtration demonstrated that the duodenal mucosa of both the human and pig contained a calcium binding protein with a similar molecular weight to the reported vitamin D dependent rat CaBP (M.W. 12 000–13 000) but dissimilar to chick CaBP (M.W. 24 000–28 000). In addition the rat, pig, and human mucosa contained a high molecular weight calcium binding protein which is probably not vitamin D dependent.A relatively simple procedure, utilizing the tagging of CaBP by 47Ca, has been developed to partially purify normal pig CaBP by Sephadex gel filtration. Further fractionation of the 12 000–13 000 M.W. area, using disc electrophoretic procedures, separated two calcium binding proteins which had similar electrophoretic mobilities and calcium binding formation constants (3.5 and 5.5 × 106, respectively), indicating that both are forms of CaBP but that either one or both have been altered during the procedures. The electrophoretic mobilities of both of these proteins are relatively low in the presence of calcium ions but much greater when calcium ions are removed by chelation with EDTA. This finding should facilitate both the identification and purification of mammalian CaBP.

LACK OF EFFECT OF OVARIECTOMY ON THE METABOLISM OF VITAMIN D AND INTESTINAL CALCIUM-BINDING PROTEIN IN FEMALE RATS

1980 ◽  
Vol 86 (3) ◽  
pp. 419-424 ◽  
Author(s):  
H. PAVLOVITCH ◽  
T. L. CLEMENS ◽  
D. LAOUARI ◽  
J. L. H. O'RIORDAN ◽  
S. BALSAN
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Ovarian Hormones ◽  
Duodenal Mucosa ◽  
Calcium Binding Protein ◽  
Egg Laying ◽  
Female Rats ◽  
Ovariectomized Rats ◽  
Calcium Stress ◽  
Pregnancy And Lactation

The metabolism of 25-hydroxycholecalciferol (25-(OH)D3), plasma concentration of 1,25-dihydroxycholecalciferol (1,25-(OH)2D3) and the amount of calcium-binding protein (CaBP) in duodenal mucosa were determined in ovariectomized rats and were compared with data observed in normal age-matched cyclic rats. Sephadex LH-20 and high-pressure liquid chromatography were used for the study of the metabolism of 25-(OH)D3. The concentration of 1,25-(OH)2D3 in plasma and prolactin in serum were measured by radioimmunoassay. Calcium-binding protein in duodenal mucosa was determined immunologically using electroimmunodiffusion. The results showed that the lack of ovarian hormones and low prolactin levels observed in ovariectomized rats did not promote a significant change in the metabolism of 25-(OH)D3, in the levels of 1,25-(OH)2D3 in the circulation or in the amount of CaBP in duodenal mucosa. It is possible that the regulation of 25-(OH)D3 by sex hormones is restricted to the state of calcium stress such as during egg-laying in birds or pregnancy and lactation in mammals.

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