scholarly journals Post-Embryonic Development and Genital-Complex Formation in Three Species of Polyclad Flatworms

2018 ◽  
Vol 35 (1) ◽  
pp. 28 ◽  
Author(s):  
Nozomi Morita ◽  
Kazuo Inaba ◽  
Yasunori Saito
Keyword(s):  
Complex Formation ◽  
Embryonic Development ◽  
Genital Complex ◽  
Polyclad Flatworms

Insemination and embryonic development of some Mediterranean polyclad flatworms

2012 ◽  
Vol 56 (4) ◽  
pp. 272-286 ◽  
Author(s):  
Mehrez Gammoudi ◽  
Carolina Noreña ◽  
Saïda Tekaya ◽  
Veronika Prantl ◽  
Bernhard Egger
Keyword(s):  
Embryonic Development ◽  
Polyclad Flatworms

Live Confocal Analysis of Fertilization and Early Development

2001 ◽  
Vol 7 (S2) ◽  
pp. 1012-1013
Author(s):  
Uyen Tram ◽  
William Sullivan
Keyword(s):  
Drosophila Melanogaster ◽  
Embryonic Development ◽  
Real Time ◽  
Early Development ◽  
Fluorescent Probes ◽  
Primary Defect ◽  
Fluorescent Analysis ◽  
Dynamic Event ◽  
Enormous Amount ◽  
Fluorescent Studies

Embryonic development is a dynamic event and is best studied in live animals in real time. Much of our knowledge of the early events of embryogenesis, however, comes from immunofluourescent analysis of fixed embryos. While these studies provide an enormous amount of information about the organization of different structures during development, they can give only a static glimpse of a very dynamic event. More recently real-time fluorescent studies of living embryos have become much more routine and have given new insights to how different structures and organelles (chromosomes, centrosomes, cytoskeleton, etc.) are coordinately regulated. This is in large part due to the development of commercially available fluorescent probes, GFP technology, and newly developed sensitive fluorescent microscopes. For example, live confocal fluorescent analysis proved essential in determining the primary defect in mutations that disrupt early nuclear divisions in Drosophila melanogaster. For organisms in which GPF transgenics is not available, fluorescent probes that label DNA, microtubules, and actin are available for microinjection.

ADHD therapy with methylphenidate in mothers – a danger for embryonic development?

2014 ◽  
Vol 47 (06) ◽  
Author(s):  
N Bergemann ◽  
K Boyle ◽  
WE Paulus
Keyword(s):  
Embryonic Development

Comparative Labelling and Biokinetic Studies of 99mTc-EDTA(Sn) and 99mTc-DTPA(Sn)

1977 ◽  
Vol 16 (01) ◽  
pp. 30-35 ◽  
Author(s):  
N. Agha ◽  
R. B. R. Persson
Keyword(s):  
Complex Formation ◽  
Significant Influence ◽  
Room Temperature ◽  
Ph Value ◽  
Maximum Activity ◽  
Reduction Step ◽  
Labelling Yield ◽  
Different Temperatures ◽  
Kinetics Of

SummaryGelchromatography column scanning has been used to study the fractions of 99mTc-pertechnetate, 99mTcchelate and reduced hydrolyzed 99mTc in preparations of 99mTc-EDTA(Sn) and 99mTc-DTPA(Sn). The labelling yield of 99mTc-EDTA(Sn) chelate was as high as 90—95% when 100 μmol EDTA · H4 and 0.5 (Amol SnCl2 was incubated with 10 ml 99mTceluate for 30—60 min at room temperature. The study of the influence of the pH-value on the fraction of 99mTc-EDTA shows that pH 2.8—2.9 gave the best labelling yield. In a comparative study of the labelling kinetics of 99mTc-EDTA(Sn) and 99mTc- DTPA(Sn) at different temperatures (7, 22 and 37°C), no significant influence on the reduction step was found. The rate constant for complex formation, however, increased more rapidly with increased temperature for 99mTc-DTPA(Sn). At room temperature only a few minutes was required to achieve a high labelling yield with 99mTc-DTPA(Sn) whereas about 60 min was required for 99mTc-EDTA(Sn). Comparative biokinetic studies in rabbits showed that the maximum activity in kidneys is achieved after 12 min with 99mTc-EDTA(Sn) but already after 6 min with 99mTc-DTPA(Sn). The long-term disappearance of 99mTc-DTPA(Sn) from the kidneys is about five times faster than that for 99mTc-EDTA(Sn).

Inactivation of α- and β-Thrombin by Antithrombin-III and Heparin

1976 ◽  
Vol 36 (03) ◽  
pp. 503-508 ◽  
Author(s):  
Raymund Machovich ◽  
György Blaskó ◽  
Anna Borsodi
Keyword(s):  
Heat Treatment ◽  
Complex Formation ◽  
Blood Circulation ◽  
Antithrombin Iii

SummaryInactivation of α- and β-thrombin by antithrombin-III and heparin was studied, since it had been suggested that two forms of thrombin exist with respect to heparin sensitivity (Machovich 1975b).It was found that the inactivation rates of α- and β-thrombin by antithrombin were different, namely α-thrombin was more sensitive to antithrombin than β-thrombin. Heparin facilitated the complex formation between α-thrombin and antithrombin-III, whereas β-thrombin inactivation was only slightly affected.Furthermore, heparin protected α-thrombin against the inactivating effect of heat, while β-thrombin lost its activity during the heat treatment.These findings suggest that the formation of β-thrombin in blood circulation may have an important role in thrombosis predisposition.

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