Thermodynamics of chain-molecule mixtures : heats of mixing of linear methylsiloxanes

1968 ◽  
Vol 64 ◽  
pp. 648 ◽  
Author(s):  
D. Patterson ◽  
S. N. Bhattacharyya ◽  
P. Picker
Keyword(s):  
Chain Molecule ◽  
Heats Of Mixing

Functional Characterization of a Variant Factor XII (F XII Locarno) in a Cross Reacting Material Positive F XII Deficient Plasma

1992 ◽  
Vol 67 (02) ◽  
pp. 219-225 ◽  
Author(s):  
Walter A Wuillemin ◽  
Miha Furlan ◽  
Hans Stricker ◽  
Bernhard Lämmle
Keyword(s):  
Dextran Sulfate ◽  
Functional Characterization ◽  
Healthy Woman ◽  
Chain Molecule ◽  
Plasma Kallikrein ◽  
Factor Xii ◽  
Single Chain ◽  
Sulfate Adsorption ◽  
Prolonged Incubation ◽  
Functional Studies

SummaryThe plasma of a healthy woman was found to contain half normal factor XII (FXII) antigen level (0.46 U/ml) without any FXII clotting activity (<0.01 U/ml). The variant FXII in this plasma, denoted as FXII Locarno, was partially characterized by immunological and functional studies on the proposita’s plasma. FXII Locarno is a single chain molecule with the same size (M r = 80 kDa) as normal FXII. Isoelectric focusing suggested an excess of negative charge in the variant FXII as compared to normal FXII. In contrast to FXII in normal plasma, FXII Locarno was not proteolytically cleaved upon prolonged incubation of proposita’s plasma with dextran sulfate. Adsorption to kaolin was similar for both, abnormal and normal FXII. Incubation of the proposita’s plasma with dextran sulfate and exogenous plasma kallikrein showed normal cleavage of FXII Locarno outside of the tentative disulfide loop Cys340-Cys467, but only partial cleavage within this disulfide loop. Furthermore, plasma kallikrein-cleaved abnormal FXII showed neither amidolytic activity nor proteolytic activity against factor XI and plasma prekallikrein.These results suggest a structural alteration of FXII Locarno, affecting the plasma kallikrein cleavage site Arg353-Val354 and thus formation of activated FXII (a-FXIIa).

Heats of mixing of butanone and chloroform with alkanes: Ternary systems

1978 ◽  
Vol 43 (3) ◽  
pp. 837-847 ◽  
Author(s):  
Julius Pouchlý ◽  
Antonín Živný ◽  
Ján Biroš
Keyword(s):  
Ternary Systems ◽  
Heats Of Mixing

Heats of mixing of butanone and chloroform with alkanes: Binary systems

1978 ◽  
Vol 43 (3) ◽  
pp. 829-836 ◽  
Author(s):  
Ján Biroš ◽  
Antonín Živný ◽  
Julius Pouchlý
Keyword(s):  
Binary Systems ◽  
Heats Of Mixing

Interpretation of heats of mixing of 1-butanol, 2-butanol and 2-methyl-2-propanol with cyclohexane in terms of some models of continuously associated solution

1984 ◽  
Vol 49 (6) ◽  
pp. 1334-1341 ◽  
Author(s):  
František Veselý ◽  
Vladimír Dohnal ◽  
Miriam Valentová ◽  
Jiří Pick
Keyword(s):  
Temperature Dependence ◽  
Interaction Parameters ◽  
Heats Of Mixing ◽  
Linear Association ◽  
Two Systems ◽  
Associated Solution

Three models of continuously associated solution complemented by an assumption of polynomial temperature dependence of corresponding interaction parameters were used for simultaneous description of the concentration and temperature dependence of heats of mixing of 1-butanol, 2-butanol and 2-methyl-2-propanol with cyclohexane. Very good results were reached for the first two systems where the Liebermann and Wilhelm model has proved to be the most suitable. With respect to the probable existence of cyclic associates in solutions of 2-methyl-2-propanol, none of the used models which assume only linear association satisfied to the extent required.

Influence of the solvent on the conformation of a chain molecule

1998 ◽  
Vol 109 (5) ◽  
pp. 2011-2022 ◽  
Author(s):  
Hin Hark Gan ◽  
Byung Chan Eu
Keyword(s):  
Chain Molecule ◽  
A Chain

scholarly journals Translational Fusion of Two β-Subunits of Human Chorionic Gonadotropin Results in Production of a Novel Antagonist of the Hormone

Endocrinology ◽  
2007 ◽  
Vol 148 (8) ◽  
pp. 3977-3986 ◽  
Author(s):  
Satarupa Roy ◽  
Sunita Setlur ◽  
Rupali A. Gadkari ◽  
H. N. Krishnamurthy ◽  
Rajan R. Dighe
Keyword(s):  
Chorionic Gonadotropin ◽  
Human Chorionic Gonadotropin ◽  
Expression System ◽  
Biologically Active ◽  
Chain Molecule ◽  
Dependent Manner ◽  
Β Subunit ◽  
Single Chain ◽  
Α Subunit ◽  
Lh Receptor

The strategy of translationally fusing the α- and β-subunits of human chorionic gonadotropin (hCG) into a single-chain molecule has been used to produce novel analogs of hCG. Previously we reported expression of a biologically active single-chain analog hCGαβ expressed using Pichia expression system. Using the same expression system, another analog, in which the α-subunit was replaced with the second β-subunit, was expressed (hCGββ) and purified. hCGββ could bind to LH receptor with an affinity three times lower than that of hCG but failed to elicit any response. However, it could inhibit response to the hormone in vitro in a dose-dependent manner. Furthermore, it inhibited response to hCG in vivo indicating the antagonistic nature of the analog. However, it was unable to inhibit human FSH binding or response to human FSH, indicating the specificity of the effect. Characterization of hCGαβ and hCGββ using immunological tools showed alterations in the conformation of some of the epitopes, whereas others were unaltered. Unlike hCG, hCGββ interacts with two LH receptor molecules. These studies demonstrate that the presence of the second β-subunit in the single-chain molecule generated a structure that can be recognized by the receptor. However, due to the absence of α-subunit, the molecule is unable to elicit response. The strategy of fusing two β-subunits of glycoprotein hormones can be used to produce antagonists of these hormones.

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