scholarly journals Differential scanning calorimetry of α2-macroglobulin and α2-macroglobulin-proteinase complexes

1983 ◽  
Vol 209 (3) ◽  
pp. 725-730 ◽  
Author(s):  
J F Chlebowski ◽  
K Williams
Keyword(s):  
Differential Scanning Calorimetry ◽  
Transition Temperature ◽  
Subunit Interactions ◽  
Scanning Calorimetry ◽  
Thermally Induced ◽  
Structural Alterations ◽  
Novel Approach ◽  
Α2 Macroglobulin ◽  
Binding Event ◽  
Transition Enthalpy

Differential scanning calorimetry is shown to detect substantial structural alterations occurring on the association of proteinases with the serum glycoprotein alpha 2-macroglobulin. At pH 7.5, the thermally induced unfolding of the macroglobulin occurs at approx. 60 degrees C with a transition enthalpy of 17 J/g. Association of active thermolysin, trypsin and papain shifts the transition temperature to 77 degrees C (transition enthalpy 5 J/g), indicating that a substantial conformational change accompanies the binding event. The stoicheiometry of the thermolysin-alpha 2-macroglobulin association producing this change appears to be unity, implying the presence of co-operative subunit interactions in the mechanism of association. The calorimetric method provides a novel approach for the evaluation of conformational variants induced on protein-protein association or pre-existing in the purified macroglobulin.

scholarly journals Isolation of active subforms of α2-macroglobulin

1985 ◽  
Vol 229 (1) ◽  
pp. 227-232 ◽  
Author(s):  
J F Chlebowski ◽  
K Williams
Keyword(s):  
Differential Scanning Calorimetry ◽  
Anion Exchange ◽  
Functional Properties ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Scanning Calorimetry ◽  
Thermally Induced ◽  
Binding Stoichiometry ◽  
Α2 Macroglobulin ◽  
Stable Forms

Anion-exchange chromatography is shown to permit resolution and separation of subforms of the serum glycoprotein alpha 2-macroglobulin. The subforms differ dramatically in their stability as judged by differential scanning calorimetry, undergoing thermally induced unfolding at temperatures of 61 and 69 degrees C respectively. In addition, the proteinase-binding stoichiometry of the subforms differs by a factor of 2, with the more- and less-stable forms binding 2 and 1 mol of proteinase per mol of tetramer respectively. The calorimetric stability of the two forms is differentially affected on treatment with neuraminidase, suggesting that the nature of glycosylation may in part account for the observed differences in physical and functional properties.

scholarly journals Thermal analysis: basic concept of differential scanning calorimetry and thermogravimetry for beginners

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Nurul Fatahah Asyqin Zainal ◽  
Jean Marc Saiter ◽  
Suhaila Idayu Abdul Halim ◽  
Romain Lucas ◽  
Chin Han Chan
Keyword(s):  
Thermal Analysis ◽  
Differential Scanning Calorimetry ◽  
Glass Transition ◽  
Transition Temperature ◽  
Glass Transition Temperature ◽  
Commercial Application ◽  
Scanning Calorimetry ◽  
Teaching Activities ◽  
Sample Decomposition ◽  
Calibration Baseline

AbstractWe present an overview for the basic fundamental of thermal analysis, which is applicable for educational purposes, especially for lecturers at the universities, who may refer to the articles as the references to “teach” or to “lecture” to final year project students or young researchers who are working on their postgraduate projects. Description of basic instrumentation [i.e. differential scanning calorimetry (DSC) and thermogravimetry (TGA)] covers from what we should know about the instrument, calibration, baseline and samples’ signal. We also provide the step-by-step guides for the estimation of the glass transition temperature after DSC as well as examples and exercises are included, which are applicable for teaching activities. Glass transition temperature is an important property for commercial application of a polymeric material, e.g. packaging, automotive, etc. TGA is also highlighted where the analysis gives important thermal degradation information of a material to avoid sample decomposition during the DSC measurement. The step-by-step guides of the estimation of the activation energy after TGA based on Hoffman’s Arrhenius-like relationship are also provided.

Influence of Gd Addition on the Structure and Capability of Ni-Mn-In Metamagnetic Shape Memory Alloys

2012 ◽  
Vol 535-537 ◽  
pp. 950-953
Author(s):  
Li Na Bai ◽  
Gui Xing Zheng ◽  
Zhi Jian Duan ◽  
Jian Jun Zhang
Keyword(s):  
Differential Scanning Calorimetry ◽  
Magnetic Properties ◽  
Magnetic Property ◽  
Transition Temperature ◽  
Martensitic Transformation ◽  
Room Temperature ◽  
Vibrating Sample Magnetometry ◽  
X Ray Diffraction ◽  
Scanning Calorimetry ◽  
X Ray

The influences of Gd concentration on martensitic transformation and magnetic properties of NiMnIn alloys were investigated by differential scanning calorimetry (DSC) , vibrating sample magnetometry (VSM), X-ray diffraction (XRD) and etc. It is Observed through the experiment: the addition of Gd enhances martensite transition temperature;X-ray diffraction analysis of experimental alloys is revealed that to the mixture is martensite and austenite at room temperature; content of Gd is not proportional to the improvement of magnetic property.

A Novel Approach to Unzipped Tubes Synthesis Using Sulfanilic Acid as the Backbone Amino Acid

2019 ◽  
Vol 57 ◽  
pp. 17-30
Author(s):  
Christopher Narh ◽  
Charles Frimpong ◽  
Qu Fu Wei
Keyword(s):  
Differential Scanning Calorimetry ◽  
Bond Formation ◽  
Sulfanilic Acid ◽  
Test Results ◽  
X Ray Diffraction ◽  
Scanning Calorimetry ◽  
Torsion Angles ◽  
X Ray ◽  
Novel Approach ◽  
Hydrophobic Peptide

In this research, unzipped sulfanilic acid inspired hydrophobic peptide tube was synthesis by increasing the polarity of sulfanilic acid through nucleophilic attachment of aniline which then provided two reactive sites at the S-terminus. These two sites were then attached with the N-terminal of valine and alanine respectively at an intensity of 1000-1600 of 11 2θ (°). Through π-π stacking at the side chains, the opened ended peptide was linearly arranged to form the unzipped tube. Fourier transform infrared spectroscopy (FTIR) confirm the amine bond formation whiles X-ray diffraction test results confirmed D-spacing 7.36 and 4.44 corresponding 2θ (°)12 and 19.97 respectively whiles the torsion angles (Ø2) conformations was between-150.5°and-169.2° and-2 between-129.0° and-150.6°. The Thermogravimetric analysis result showed an increase in the rigidity of the bond with an increasing intensity. Finally, Differential scanning calorimetry (DSC) test was carried out to confirm the crystallinity of the structure. Keywords: Sulfanilic acid, hydrophobic Peptide, Unzipped tubes, Nanomaterial

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