Utilization of steel plates from abolished old metallurgical factory for shielding of low activity measurement devices

1988 ◽  
Vol 126 (5) ◽  
pp. 351-352
Author(s):  
Z. Řanda
Keyword(s):  
Steel Plates ◽  
Activity Measurement ◽  
Metallurgical Factory ◽  
Measurement Devices ◽  
Low Activity

The Carboxyl-Terminal Domains of ADAMTS13 Cause Substrate-Dependent Divergence of ADAMTS13 Activity.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 381-381
Author(s):  
Wenhua Zhou ◽  
Han-Mou Tsai
Keyword(s):  
Mouse Liver ◽  
Mdck Cells ◽  
Repeat Sequence ◽  
Full Length ◽  
Carboxyl Terminus ◽  
Mouse Strains ◽  
Pcr Analysis ◽  
Activity Measurement ◽  
Affected Mouse ◽  
Low Activity

ADAMTS13, a circulating metalloprotease that cleaves the Y1605-M1606 bond of VWF, is critical for preventing intravascular platelet thrombosis of thrombotic thrombocytopenic purpura. Unlike genetic deficiency of ADAMTS13 in patients, inactivation of ADAMTS13 created by homologous recombination causes either no or delayed-onset phenotypic abnormalities in mice, depending on the strains examined. In order to further understand the role of ADAMTS13 in VWF homeostasis, we investigated the structure and function of the enzyme in various mouse strains. As in human subjects, RT PCR analysis revealed that ADAMTS13 was expressed primarily in the mouse liver. However, the enzyme activity levels of mouse plasma ADAMTS13 segregated in two groups: a low group (C56BL/6J strain, 24%±10% of normal human plasma, N=21; and DBA/2J strain, 24%±7%, N=6), and a high group (FVB/NJ strain, 288%±60%, N=23; and 129×1/SvJ strain, 313%±39%, N=6). No such difference was detected when GST-His fusion or FRET form of VWF73 (D1596-R1668) peptide was used for activity measurement. Real-time analysis of RNA extracted from mouse livers showed that the ADAMTS13 transcript levels were similar between the two groups. Cloning of the mouse liver ADAMTS13 yielded a predominant 3.5kb instead of the expected 4.3kb species from the low-activity group. This truncated cDNA contained the first 23 exons of the full-length (FL) ADAMTS13 and an extraneous sequence derived from the long terminal repeat sequence of a previously described IAP-type retrotransposone located in intron 23 of affected mouse genome. Protein expression analysis of the cloned cDNA in HEK 293 and MDCK cells showed that both full-length and IAP-type ADAMTS13 proteins were secreted efficiently without evidence of polarity. Nevertheless, the IAP-type ADAMTS13 was only 10% as active as FL ADAMTS13 in cleaving VWF multimers, but was 50% – 70% as effective in cleaving human or mouse VWF73 peptides, suggesting that truncation and/or presence of IAP sequence at the C-terminus sequence of ADAMTS13 markedly impeded cleavage of VWF multimers. Crossbreeding between C57BL/6J and FVB/NJ strains of mice confirmed that the low-activity phenotype was linked to homozygous IAP genotype. In SDS agarose gel analysis, both C57BL/6J and FVB/NJ strains contained ultra large multimers similar to those observed in ADAMTS13-null mice (kindly provided by D. Motto and D. Ginsburg). Analysis of recombinant human ADAMTS13 proteins also showed that proteins truncated at the disintegrin or spacer domain were relatively more active in cleaving VWF peptide substrates than cleaving VWF multimers. In conclusion, the presence of an IAP-type retrotransposone in the ADAMTS13 gene enhances alternative splicing, resulting in predominant expression of IAP types of ADAMTS13 in the affected mouse strains. Nevertheless, ADAMTS13 does not regulate VWF multimer size, and deficiency of ADAMTS13 is phenotypically silent in the mice examined. The carboxyl-terminus sequence of ADAMTS13 may enhance interaction with VWF multimers and its subsequent cleavage. Clinically, ADAMTS13 assay results should be interpreted with caution when VWF peptide-based proteins are used as the substrate, because they yield higher activity values for ADAMTS13 proteins lacking the carboxyl terminus sequence.

Windowless counter for low activity measurement

1953 ◽  
Vol 30 (11) ◽  
pp. 439-439
Author(s):  
The Atomic Center for Instruments a Inc.
Keyword(s):  
Activity Measurement ◽  
Low Activity

Wearable Physical Activity Measurement Devices Used in Arthritis

2020 ◽  
Vol 72 (S10) ◽  
pp. 703-716
Author(s):  
Jasmin K. Ma ◽  
Amber Chan ◽  
Amrit Sandhu ◽  
Linda C. Li
Keyword(s):  
Physical Activity ◽  
Activity Measurement ◽  
Physical Activity Measurement ◽  
Measurement Devices

A Comparison of the in Vitro and in Vivo Thrombogenic Activity of Factor IX Concentrates Using Stasis (Wessler) and Non-Stasis Rabbit Models

1980 ◽  
Vol 44 (02) ◽  
pp. 081-086 ◽  
Author(s):  
C V Prowse ◽  
A E Williams
Keyword(s):  
Platelet Rich Plasma ◽  
Thrombus Formation ◽  
Factor Ix ◽  
Coagulation System ◽  
In Vitro Tests ◽  
Clinical Use ◽  
Low Activity

SummaryThe thrombogenic effects of selected factor IX concentrates were evaluated in two rabbit models; the Wessler stasis model and a novel non-stasis model. Concentrates active in either the NAPTT or TGt50 in vitro tests of potential thrombogenicity, or both, caused thrombus formation in the Wessler technique and activation of the coagulation system in the non-stasis model. A concentrate with low activity in both in vitro tests did not have thrombogenic effects in vivo, at the chosen dose. Results in the non-stasis model suggested that the thrombogenic effects of factor IX concentrates may occur by at least two mechanisms. A concentrate prepared from platelet-rich plasma and a pyrogenic concentrate were also tested and found to have no thrombogenic effect in vivo.These studies justify the use of the NAPTT and TGt50 in vitro tests for the screening of factor IX concentrates prior to clinical use.

Separation of Heparin into Subtractions by DEAE-Cellulose Chromatography

1979 ◽  
Vol 42 (05) ◽  
pp. 1452-1459 ◽  
Author(s):  
Robert H Yue ◽  
Toby Starr ◽  
Menard M Gertler
Keyword(s):  
High Activity ◽  
Uronic Acid ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
Net Charge ◽  
Uronic Acid Content ◽  
Successful Separation ◽  
Salt Gradient ◽  
Structure And Activity ◽  
Low Activity

SummaryCommercial porcine heparin can be separated into three distinct subtractions by using DEAE-cellulose chromatography and a stepped salt gradient. Gram quantities of heparin can be fractionated by this technique. All three heparin subtractions can accelerate the inhibition of thrombin by antithrombin III with different efficiency. The specific activities of the high activity heparin, intermediate activity heparin and low activity heparin are 228 units/mg, 142 units/mg and 95 units/mg, respectively. Both the uronic acid content and the quantity of N-SO4 for all three heparin subfractions have been evaluated. The high activity heparin has the lowest uronic acid and N-SO4 content. The successful separation of commercial heparin into three distinct subfractions by means of ion-exchange chromatography suggests that the net charge on these three heparin components will serve as a model system in the elucidation of the structure and activity relationship to the biological function of heparin.

Determination of Factor XIII Activity and of Factor XIII Inhibitors Using an Ammonium-Sensitive Electrode

1983 ◽  
Vol 50 (02) ◽  
pp. 563-566 ◽  
Author(s):  
P Hellstern ◽  
K Schilz ◽  
G von Blohn ◽  
E Wenzel
Keyword(s):  
Factor Xiii ◽  
Normal Subjects ◽  
The Other ◽  
Activity Measurement ◽  
Factor Xiii Deficiency ◽  
Assay Procedure ◽  
Stabilization Factor ◽  
Release Method ◽  
Sensitive Electrode

SummaryAn assay for rapid factor XIII activity measurement has been developed based on the determination of the ammonium released during fibrin stabilization. Factor XIII was activated by thrombin and calcium. Ammonium was measured by an ammonium-sensitive electrode. It was demonstrated that the assay procedure yields accurate and precise results and that factor XIII-catalyzed fibrin stabilization can be measured kinetically. The amount of ammonium released during the first 90 min of fibrin stabilization was found to be 7.8 ± 0.5 moles per mole fibrinogen, which is in agreement with the findings of other authors. In 15 normal subjects and in 15 patients suffering from diseases with suspected factor XIII deficiency there was a satisfactory correlation between the results obtained by the “ammonium-release-method”, Bohn’s method, and the immunological assay (r1 = 0.65; r2= 0.70; p<0.01). In 3 of 5 patients with paraproteinemias the values of factor XIII activity determined by the ammonium-release method were markedly lower than those estimated by the other methods. It could be shown that inhibitor mechanisms were responsible for these discrepancies.

Metrological support of individual blood glucose meters in telemedicine

2019 ◽  
pp. 52-56
Author(s):  
Yu.F. Glukhov ◽  
N.V. Krutikov ◽  
A.V. Ivanov ◽  
N.P. Muravskaya
Keyword(s):  
Blood Glucose ◽  
Blood Glucose Level ◽  
Glucose Level ◽  
Measurement Data ◽  
Test Method ◽  
Level Measurement ◽  
Measurement Devices ◽  
Real Practice ◽  
Health Care Centers ◽  
Medical Measurement

We have studied and analyzed status and metrological supervision of blood glucose monitors, individual devices for a person’s blood glucose level measurement. It has been indicated that nowadays blood glucose monitors like other individual devices for medical measurement are not allowed to be involved in telemedicine public service. This accounts for absence of metrological supervision with these measurement devices in telemedicine. In addition, the key problem is absence of safe methods and means of remote verificaition, calibration and transmission of measurement data to health care centers. The article offers a remote test method for blood glucose monitors using a number of resistors with values correlating with measured blood glucose level. The available method has been successfully trialed in real practice.

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