scholarly journals Chemical differences between thyrotropin isohormones

1977 ◽  
Vol 167 (1) ◽  
pp. 279-280 ◽  
Author(s):  
K M M Davy ◽  
J S Fawcett ◽  
C J O R Morris

Amide determinations have been carried out, with a newly developed g.l.c. method, on thyrotropin hormones prepared by isoelectric focusing. The observed differences in amide content fully account for the differences in the electrochemical properties of the isohormones.

1977 ◽  
Vol 38 (02) ◽  
pp. 0475-0485 ◽  
Author(s):  
Anna D. Borsodi ◽  
Ralph A. Bradshaw

SummaryThe plasma of individuals, hetero- or homozygous for α1-antitrypsin deficiency, contains greatly decreased amounts of antithrombin activity as assayed against factor Xa. However, heparin stimulation of the residual antithrombin activity is observed, which is comparable to that of normal plasma. Antithrombins isolated from both normal and α1-antitrypsin deficient plasma by a simplified procedure are indistinguishable in both properties and yields. The microheterogeneity observed on isoelectric focusing of both preparations can be eliminated by treatment with neuraminidase. Neither purified human antithrombin nor α1-antitrypsin, when assayed against bovine trypsin, is stimulated by heparin. These results clearly establish the unique natures of antithrombin and α1-antitrypsin and show that about 75% of the antithrombin activity measured in normal plasma is due to α1-antitrypsin. Estimates of anti thrombin III activity in normal plasma by assays dependent on enzymatic activity can probably be obtained only in the presence of heparin.


1973 ◽  
Vol 73 (3) ◽  
pp. 483-488 ◽  
Author(s):  
F. Adlkofer ◽  
H. Schleusener ◽  
L. Uher ◽  
A. Ananos ◽  
C. Brammeier

ABSTRACT Crude IgG of sera from 3 patients with Graves' disease, which contained LATS-activity and/or thyroid antibodies, was fractionated by isoelectric focusing in a pH-range between 6.0 to 10.0. LATS-activity was found in IgG-subfractions from pH 7.5 to 9.5, thyroglobulin antibodies and thyroid microsomal antibodies from pH 6.0 to 10.0. It was not possible to separate LATS-activity from the thyroid antibodies by this technique. The results indicate that LATS and the thyroid antibodies are heterogeneous and of polyclonal origin.


1971 ◽  
Vol 68 (1_Supplb) ◽  
pp. S15
Author(s):  
F. Adlkofer ◽  
H. Schleusener ◽  
L. Uher ◽  
H. J. Kirstaedter

2020 ◽  
Author(s):  
Thomas Baumgartner ◽  
Paul Demay-Drouhard

The unexpectedly challenging synthesis of 4-pyridyl-extended dithienophospholes is reported. The optical and electrochemical properties of the phosphoryl-bridged species were studied experimentally and computationally, and their properties compared to their non-<i>P</i>-bridged congeners. The 4-pyridyl-extended dithieno-phospholes display quantitative luminescence quantum yields in solution.<br><br>


2020 ◽  
Author(s):  
Thomas Baumgartner ◽  
Paul Demay-Drouhard

The unexpectedly challenging synthesis of 4-pyridyl-extended dithienophospholes is reported. The optical and electrochemical properties of the phosphoryl-bridged species were studied experimentally and computationally, and their properties compared to their non-<i>P</i>-bridged congeners. The 4-pyridyl-extended dithieno-phospholes display quantitative luminescence quantum yields in solution.<br><br>


2016 ◽  
Vol 15 (5) ◽  
pp. 955-963 ◽  
Author(s):  
Corneliu Munteanu ◽  
Bogdan Istrate ◽  
Daniel Mareci ◽  
Sergiu Stanciu ◽  
Carmen-Iulia Crimu ◽  
...  

2014 ◽  
Vol 13 (8) ◽  
pp. 1987-1995 ◽  
Author(s):  
Liviu-Virgil Costea ◽  
Gunter Fafilek ◽  
Hermann Kronberger

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