Specific activities of Poetam preparation (superlow-doses of antibodies to erythropoietin) and recombinant erythropoietin

2006 ◽  
Vol 142 (3) ◽  
pp. 320-323
Author(s):  
A. M. Dygai ◽  
V. V. Zhdanov ◽  
E. V. Udut ◽  
E. V. Simanina ◽  
L. A. Gur’yantseva ◽  
...  
1993 ◽  
Vol 69 (05) ◽  
pp. 430-435 ◽  
Author(s):  
Colin Longstaff ◽  
Man-Yu Wong ◽  
Patrick J Gaffney

SummaryAn international collaborative study has been carried out to investigate the reproducibility of hirudin assays in 13 laboratories using four recombinant hirudins and one natural, sulphated product. A simple assay procedure was proposed involving the titration of α-thrombin with inhibitor and measurement of residual activity using a chromogenic substrate. A standard α-thrombin preparation was supplied to ensure that this reagent was of uniform quality throughout the study. The method appeared to present no difficulties and laboratories reported similar potencies for the 5 hirudin samples, in line with expected values. This gave 200–222 Thrombin Inhibitory Units/ampoule (TIU/ampoule) of lyophilised hirudin, with geometric coefficient of variation (gcv) values ranging from 10.15–15.97%. This corresponds to specific activities of approximately 14,300–15,900 TIU/mg protein. This is close to the upper limit of previously reported values of specific activity. We conclude that the precision of this determination compared with the wider range of values in the literature (8,000–16,000 thrombin inhibitory units [TIU]/mg) results from the use of good quality standard α-thrombin by all laboratories. This study has important implications for hirudin standardisation.


1996 ◽  
Vol 76 (03) ◽  
pp. 361-368 ◽  
Author(s):  
Carrie H Fang ◽  
T-C Lin ◽  
Arabinda Guha ◽  
Yale Nemerson ◽  
William H Konigsberg

SummaryIn an attempt to define sequence elements in human and mouse tissue factor (TF) that are responsible for the species specificity observed in their interaction with human factor VIIa (HVIIa), we constructed human-mouse chimeric TF cDNAs, inserted them into plasmid vectors, and induced their expression in E.coli. Assays for procoagulant activity were carried out with the resulting E. coli lysates using (HVIIa) human and mouse (MVIIa). The ratio of the procoagulant activities, HVIIa/MVIIa, revealed that human TF exon 3 was essential for activity when the TF:VIIa complex was formed with HVIIa. By ligating the maltose binding protein (MBP) gene to TF cDNAs it was possible to construct, express and purify MBP-TF chimeras as well as to estimate their specific activities. With selected MBP-TF chimeras and HVIIa we determined kinetic parameters for the activation of human factor X. Replacement of exon 3 in human TF cDNA with the corresponding exon from mouse TF cDNA resulted in both lower affinity for HVIIa and failure to convert bound HVIIa into a potent protease


1972 ◽  
Vol 71 (1) ◽  
pp. 24-36 ◽  
Author(s):  
Ariel Gordin ◽  
Pirkko Saarinen

ABSTRACT An account is given of a methodological study of the double-antibody radioimmunoassay of human TSH, using highly purified labelled human TSH as tracer. It was shown that conventional paper electrophoresis was not adequate for studying the purity of labelled human TSH. When polyvinylchloride (Pevikon®) electrophoresis was used, four subfractions could still be separated, even though, on paper electrophoresis, the material seemed to be homogeneous. Only two of the four Pevikon fractions were immunoreactive. Purification of labelled human TSH by Pevikon electrophoresis also improved the sensitivity of the assay. Specific activities of about 100 mCi/mg gave the highest initial binding capacity, produced least damage to the labelled hormone and showed the best stability of the tracer without influencing the sensitivity of the method. In different storage conditions, labelled human TSH was found to be most stable at −20°C and diluted 1/100. Only in pregnancy did the addition of HCG seem necessary. The mean TSH value in healthy subjects was 3.6 ± 1.4 μU/ml (mean±sd) with a range from 1.6 μU/ml to 8.8 μU/ml.


1969 ◽  
Vol 62 (1_Suppl) ◽  
pp. S134-S144 ◽  
Author(s):  
W. M. Hunter

ABSTRACT The preparation of radioiodinated human LH and human FSH with specific activities of 50—150 μc/μg for use in specific radioimmunoassay systems is described. Methods for minimising iodination damage, for removing severely damaged fractions after iodination and for assessing the immunological reactivity of the final products are detailed. The obligation upon immunoassayists to demonstrate that their labelled preparations do indeed represent the hormones under consideration is discussed and criteria which may contribute evidence on this question are put forward.


2018 ◽  
Vol 28 (6) ◽  
pp. 2067-2073
Author(s):  
Iliyan Rizov

The report presents a model for mobile social work with families, which develops in Roma communities (Varna Municipality and Aksakovo Municipality) for 10 years. This model seeks to resolve the problem about inefficiency of institutions in their work to reduce the number of abandoned children and to increase child well-being in vulnerable communities. There are presented specific activities and results, what show a way of support of the process for deinstitutionalization of childcare.


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