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Assessing the Prevalence and Characteristics of Vitamin D Deficiency in Hemodialysis Patients in a Long Term Acute Care HospitalWolf, Emily A. January 2011 (has links)
No description available.
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A study of the influence of dietary vitamin A on the level of liver and serum cholinesterase in rats /Garry, Philip J. January 1974 (has links)
No description available.
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Vitamin D and K status and bone health in pediatric cystic fibrosis patientsDrury, Donna. January 2006 (has links)
No description available.
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1,25-DIHYDROXYVITAMIN D: HORMONAL REGULATION OF BIOSYNTHESIS AND PURIFICATION OF ITS INTESTINAL RECEPTORPike, John Wesley January 1979 (has links)
No description available.
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The effect of antioxidants on the stability of vitamin A in a vitamin-mineral premixPatterson, Karen Forney January 2011 (has links)
Typescript (photocopy). / Digitized by Kansas Correctional Industries
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A histological study of skeletal muscle and connective tissue in vitamin C-deficient guinea pigsTraulsen, Jessie Pelham January 2011 (has links)
Typescript, etc. / Digitized by Kansas State University Libraries
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The vitamin A content of the yolk of eggs as related to rate of productionKoenig, Myra Caroline. January 1934 (has links)
Call number: LD2668 .T4 1934 K61
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The thiamine content of raw and cooked frozen pork loinHoward, Phyllis Burtis. January 1944 (has links)
Call number: LD2668 .T4 1944 H62 / Master of Science
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Studies on effects of vitamin C-deficiency on the number of red and white cells and the hemoglobin in guinea pig bloodKordisch, Mary Schroller. January 1944 (has links)
Call number: LD2668 .T4 1944 K6 / Master of Science
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STRUCTURE - FUNCTION RELATIONSHIPS OF THE VITAMIN D HORMONE RECEPTOR.ALLEGRETTO, ELIZABETH ANNE. January 1987 (has links)
Avian intestinal cytosoluble receptors for 1,25-dihydroxyvitamin D₃ (1,25(OH)₂D₃) were subjected to limited trypsin digestion, endogenous proteolytic action, as well as carboxypeptidase treatment, and the physical and functional properties of the resulting discrete polypeptide fragments were identified and contrasted with the native 1,25(OH)₂D₃ receptor. Resultant fragments were followed by tracing either radioactive 1,25(OH)₂D₃ or by probing with anti-receptor monoclonal antibodies. Two differentially trypsin-sensitive effects on the 1,25(OH)₂D₃ receptor were noted when fragments were detected by their ability to bind 1,25(OH)₂[³H]D₃. Two hormone-bound fragments of 40 and 30 kDa were formed; neither bound to DNA-cellulose nor anti-receptor monoclonal antibodies. Immunoblot technology was used to show the disappearance of the 60 kDa receptor with increasing trypsin concentrations, paralleling the appearance of an immunoreactive 20 kDa fragment. The 20 kDa fragment did not bind hormone but was capable of interacting with DNA-cellulose in a fashion identical to that of the 60 kDa receptor. This fragment is likely the complementary fragment to the hormone-bound fragment of 40 kDa that is described above. In contrast to the exogeneous effect of trypsin, incubation of chick intestinal cytosol resulted in the time-dependent formation of an endogenous protease-derived fragment of 45 kDa. This species retained the hormone-binding site and the antibody determinant, but was devoid of DNA-binding activity. Moreover, it did not generate the trypsin-dependent 20 kDa fragment and therefore was derived from the opposite end of the receptor molecule. Carboxypeptidase treatment of the 1,25(OH)₂D₃ receptor produces a 56 kDa fragment which does not retain hormone, but which does bind to DNA-cellulose and monoclonal antibody. These combined data from various limited enzymatic cleavage studies of the receptor have facilitated the construction of a schematic model of the chick receptor in which the immunoreactive epitope is located between the N-terminal DNA-binding domain and the C-terminal hormone-binding domain. This map for the 1,25(OH)₂D₃ receptor protein is consistent with the general structure of steroid and thyroid hormone receptors and places the vitamin D hormone receptor in a class of macromolecules that are postulated to bind enhancer regions of responsive DNA and thereby control target gene transcription.
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