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1.
Comp Biochem Physiol B Biochem Mol Biol ; 165(3): 196-200, 2013 Jul.
Article in English | MEDLINE | ID: mdl-23648288

ABSTRACT

Vitamin D deficiency can lead to several health problems collectively called metabolic bone disease (MBD). One commonly kept reptile species prone to develop MBD if managed incorrectly is the bearded dragon (Pogona vitticeps). This study aimed to determine the extent to which adult female bearded dragons fed a diet low in vitamin D can use stored vitamin D and its metabolites to maintain plasma 25(OH)D(3) and 1,25(OH)(2)D(3) concentrations after discontinuing UVb exposure. Blood samples of healthy adult female bearded dragons, exposed to UVb radiation for over 6 months were collected (day 0) after which UVb exposure was discontinued for 83 days and blood was collected. Blood plasma was analysed for concentrations of total Ca, total P, ionized Ca, uric acid, 25(OH)D(3) and 1,25(OH)(2)D(3). There was no significant change in plasma 25(OH)D(3) and 1,25(OH)(2)D(3) concentrations during the study. While total Ca and P in whole blood was found to significantly decrease over time (P < 0.0088 and 0.0016, respectively), values were within the reference range. Plasma ionized Ca tended (P = 0.0525) to decrease during the study. Adult female bearded dragons, previously exposed to UVb, are able to maintain blood vitamin D metabolite concentrations when UVb exposure is discontinued for a period of up to 83 days.


Subject(s)
Cholecalciferol/blood , Cholecalciferol/metabolism , Lizards/blood , Ultraviolet Rays , Animals , Female
3.
Biochemistry ; 25(17): 4832-9, 1986 Aug 26.
Article in English | MEDLINE | ID: mdl-2945592

ABSTRACT

Intramolecular excimer formation with the fluorescent probe 1,3-di(1-pyrenyl)propane, differential scanning calorimetry, and X-ray diffraction were used to assess the effect of ethanol, 1-butanol, and 1-hexanol on the bilayer organization in model membranes, sarcoplasmic reticulum (SR) lipids and native SR membranes. These alcohols have fluidizing effects on membranes and lower the main transition temperature of dimyristoylphosphatidylcholine (DMPC), but only 1-hexanol alters the cooperativity of the phase transition and significantly increases the thickness of DMPC bilayers. The interaction of the three alcohols with the SR Ca2+ pump was also investigated. Hydrolysis of ATP and coupled Ca2+ uptake are differently sensitive to the three alcohols. Whereas ethanol and 1-butanol inhibited the Ca2+ uptake, 1-hexanol stimulated it. Nevertheless, the energetic efficiency of the pump (Ca2+/ATP) is not significantly affected by ethanol or 1-hexanol, but uncoupling was observed with 1-butanol at high concentrations. The different effects of alcohols on the activity of SR membranes rule out an unitary mechanism of action on the basis of fluidity changes induced in the lipid bilayer. Depending on the chain length, the alcohols interact with the SR membranes in different domains, perturbing differently the Ca2+-pump activity.


Subject(s)
Alcohols/pharmacology , Membrane Fluidity/drug effects , Sarcoplasmic Reticulum/metabolism , Animals , Biological Transport, Active/drug effects , Calcium-Transporting ATPases/metabolism , Calorimetry, Differential Scanning , Kinetics , Lipid Bilayers , Liposomes , Muscles/metabolism , Rabbits , Sarcoplasmic Reticulum/drug effects , Spectrometry, Fluorescence , Structure-Activity Relationship , X-Ray Diffraction
4.
Biochim Biophys Acta ; 821(1): 165-8, 1985 Nov 21.
Article in English | MEDLINE | ID: mdl-4063357

ABSTRACT

The influence of sucrose, between 0 and 70% in the aqueous phase, upon multilamellar liposomes of dimyristoylphosphatidylcholine was examined by differential scanning calorimetry and X-ray diffraction analysis. Increasing concentrations of sucrose increase the temperatures of both the main transition and the pretransition of the lipid. The effect is greater on the pretransition than on the main transition. At 35 degrees C the interlamellar spacing in the multilamellar liposomes is reduced by increasing sucrose concentration in the aqueous phase and no significant effects are seen in the chain lattice of the bilayers. This result is interpreted as a dehydrating effect of sucrose upon the bilayer-water system at 35 degrees C. At 5 degrees C the interlamellar spacing is increased and this increase is, at high (70%) sucrose concentrations, attributable to an untilting of the lipid acyl chains with no change in the thickness of the aqueous layers in the multilamellae.


Subject(s)
Lipid Bilayers , Phosphatidylcholines , Sucrose , Calorimetry, Differential Scanning , Models, Biological , Molecular Conformation , X-Ray Diffraction
5.
Biochim Biophys Acta ; 733(2): 201-9, 1983 Sep 07.
Article in English | MEDLINE | ID: mdl-6882759

ABSTRACT

Polarized infrared spectra of melittin incorporated into macroscopically oriented lipid membranes are reported. From the linear dichroism of the amide I and amide II vibrational bands, the spatial orientation of the melittin helices was determined as being preferentially parallel to the membrane normal, under our experimental condition of low water content and an ordered lipid phase. Considering the various models for the orientation of melittin in lipid membranes proposed in the literature, we conclude that our data are in accord with an arrangement whereby the hydrophobic part of the polypeptide either spans the bilayer in the form of two bent helix segments, or is folded back within one monolayer in the form of a wedge.


Subject(s)
Bee Venoms , Lipid Bilayers , Melitten , Phosphatidylcholines , Models, Biological , Molecular Conformation , Protein Conformation , Spectrophotometry, Infrared , Structure-Activity Relationship
6.
Biochim Biophys Acta ; 727(2): 246-54, 1983 Jan 19.
Article in English | MEDLINE | ID: mdl-6838869

ABSTRACT

The effect of variation of the acyl chain composition of phosphatidylcholines upon thermal behaviour of multilamellar liposomes was evaluated by calorimetry and X-ray studies. A total of thirteen different phosphatidylcholines were examined. They differed from each other in the length as well as in the position of the acyl chains in the glycerol backbone. The experimental results show that the hitherto accepted phase scheme for phosphatidylcholine-water systems is incomplete and has to be extended to include the behaviour of samples that have been stored for long times at low temperatures. The X-ray results show that the structure of the new low-temperature phase is not in agreement with the hexagonal packing of the acyl chains. To explain the X-ray results, a two-dimensional orthorhombic unit cell has to be assumed in order to fit all the observed reflexes in the wide-angle region.


Subject(s)
Liposomes , Phosphatidylcholines , Calorimetry , Molecular Conformation , Structure-Activity Relationship , X-Ray Diffraction
7.
Biochemistry ; 20(5): 1392-6, 1981 Mar 03.
Article in English | MEDLINE | ID: mdl-7225336

ABSTRACT

The translational diffusion of the integral membrane sialoglycoprotein from erythrocyte membranes, glycophorin, incorporated into bilayer membranes of dimyristoyl-phosphatidylcholine at a protein/lipid molar ratio of 1:4500 was examined by using the fluorescence redistribution after photobleaching technique. A plot of the diffusion coefficient vs. temperature shows a sharp decrease in the rate of diffusion at about 15 degrees C. This sharp diffusion transition is at a temperature some 9 degrees C lower than the calorimetrically measured lipid gel-liquid crystalline phase transition temperature of the system. The difference between the diffusion transition temperature and the lipid phase transition temperature is attributed toi a localized fluidizing effect of the protein upon the gel phase lipid. The value of the diffusion coefficient above 15 degrees C was found to be (1-2) x 10(-8) cm(2)s(-1), and below 15 degrees C it was lower than about 5 x 10(-11)cm(2)s(-1). The fluorescence recovery in the bleached area as a consequence of diffusional redistribution appeared to be due to a single diffusing species at temperatures above 15 degrees C and due to more than one diffusing species below this temperature.


Subject(s)
Glycophorins , Lipid Bilayers , Phosphatidylcholines , Sialoglycoproteins , Dimyristoylphosphatidylcholine , Erythrocyte Membrane , Humans , Kinetics , Microscopy, Fluorescence , Photolysis
8.
Biochemistry ; 20(3): 662-5, 1981 Feb 03.
Article in English | MEDLINE | ID: mdl-7213601

ABSTRACT

Aqueous dispersions of synthetic lecithins with different fatty acids in positions 1 and 2 of the glycerol molecule were studied by calorimetry. The data show that variation of the acyl chains in different positions of the glycerol backbone either have no influence upon or contribute 0.5 kcal/mol per CH2 segment to the phase transition enthalpy. Different molecular ordering of the mixed acyl chain lecithins in the bilayer is discussed in light of the results.


Subject(s)
Lipid Bilayers , Phosphatidylcholines , Calorimetry , Fatty Acids , Molecular Conformation , Structure-Activity Relationship , Water
9.
Biochim Biophys Acta ; 599(2): 464-72, 1980 Jul.
Article in English | MEDLINE | ID: mdl-7407102

ABSTRACT

The influence of pH and ionic strength on the phase transition behavior of 1,2-dihexadecylphosphatidylethanolamine was studied calorimetrically. In the range of ionic strength from 0.75 to 1.5 M NaCl at pH larger than 13, where the amino group of the phosphatidylethanolamine is in the deprotonated state, resulting in one negative charge per lipid molecule, the calorimetric scan shows a pretransition before the main transition. Accompanying freeze-fracture electron microscopic studies on these preparations in the temperature range between the pre- and main transitions show a regular suface, the so-called ripple structure. These are comparable with the structures seen in phosphatidylcholine-water systems at temperatures between the pre- and main transition.


Subject(s)
Membranes, Artificial , Phosphatidylethanolamines , Calorimetry , Freeze Fracturing , Hydrogen-Ion Concentration , Microscopy, Electron , Molecular Conformation , Osmolar Concentration , Thermodynamics
10.
Biochim Biophys Acta ; 555(3): 409-16, 1979 Aug 23.
Article in English | MEDLINE | ID: mdl-39600

ABSTRACT

The influence of pH on the structure of 1,2-(ditetradecyl)-phosphatidic acid was investigated by differential scanning calorimetry and freeze-fracture electron microscopy. At pH 13.5--14 (2.6 M K+), where phosphatidic acid has two negative charges, calorimetric scans show a small transition (pretransition) below the main phase transition temperature. Freeze-fracture studies of the same dispersions reveal regular band patterns (so-called ripples) in the plane of the bilayers, when the lipid is quenched from below the main phase transition temperature. This rippled structure is similar to the well-known rippled structure of phosphatidylcholines.


Subject(s)
Lipid Bilayers , Phosphatidic Acids , Calorimetry, Differential Scanning , Hydrogen-Ion Concentration
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