Quantum Biochemical Investigation of Lys49-PLA2 from Bothrops moojeni

Author(s):  
E. D. Barbosa ◽  
J. X. Lima Neto ◽  
K. S. Bezerra ◽  
J. I. N. Oliveira ◽  
L. D. Machado ◽  
...  
ChemBioChem ◽  
2021 ◽  
Author(s):  
Yan Zhang ◽  
Junwei An ◽  
Yifeng Wei ◽  
Jiayi Liu ◽  
Ee Lui Ang ◽  
...  

Author(s):  
Maria Isabel Müller ◽  
Enzo Emmerich ◽  
Edna Paulino de Alcantara ◽  
Letícia Pereira Ungari ◽  
Mariana Bertholdi Ebert ◽  
...  

Toxicon ◽  
2020 ◽  
Vol 177 ◽  
pp. S35-S36
Author(s):  
Nathalia Galizio ◽  
Weslei Aguiar ◽  
Tassia Chiarelli ◽  
Caroline Serino-Silva ◽  
Caroline Fabri Bittencourt Rodrigues ◽  
...  

Toxicon ◽  
2010 ◽  
Vol 55 (2-3) ◽  
pp. 343-352 ◽  
Author(s):  
Neide Galvão Nascimento ◽  
Marlos Cortez Sampaio ◽  
Renata Amaral Olivo ◽  
Catarina Teixeira

2018 ◽  
Vol 37 (9) ◽  
pp. 507-521 ◽  
Author(s):  
Yuchuan Guo ◽  
Wei Gong ◽  
Lizhen Wang ◽  
Jiatong Guo ◽  
Guoxia Jin ◽  
...  

Author(s):  
E C Attwood ◽  
G E Atkin

The thyroxine: thyroxine-binding globulin (T4: TBG) ratio is now an established part of the biochemical investigation of thyroid function. Reference ranges have been reported for euthyroid subjects with TBG levels within the range 6–16 mg/l. Routine assay of TBG on all thyroid function tests in this laboratory has suggested that, in patients with low or high TBG levels, the established reference ranges for T4:TBG may not be strictly applicable. A retrospective study has been made of a large number of thyroid function requests, including serum total T4, free T4, TBG, and TSH assays. Evidence is presented to show that in subjects with a TBG level of less than 8 mg/l the reference range for T4: TBG is elevated. Similarly, in subjects with a TBG greater than 16 mg/l, the reference range for T4: TBG is lowered. The data suggest that it is necessary to quote a T4: TBG reference range based on small increments of TBG levels or to relate total T4 reference ranges to those increments.


1976 ◽  
Vol 21 (3) ◽  
pp. 449-463
Author(s):  
A.G. Booth ◽  
J. Kenny

The vesiculation of kidney proximal tubule microvilli has been examined in tissue slices, isolated brush borders and isolated microvilli. Vesiculation could be induced in tissue slices by 2,4-dinitrophenol and anoxia. Cycloheximide and fluoride had no effect. In brush borders and microvilli, the vesiculation was found to be essentially temperature-dependent. Whilst an osmotic swelling could be produced by hypo-osmolar media, the temperature-dependent vesiculation could not be prevented in hyper-osmolar media. Of a wide variety of reagents tested, only glutaraldehyde, mercuric chloride and mersalyl were effective in arresting the vesiculation. Electron micrographs show that vesiculation involves a collapse of the internal structure of the microvillus. However, the collapse was not associated with depolymerization of the microvillus actin filaments. Rather it appeared to be due to the parting of cross-bridges between the membrane and the actin filaments. The nature of these cross-bridges is discussed: it is suggested that alpha-actinin possesses the characteristics for the cross-bridging protein and that vesiculation might be explained by the displacement of alpha-actinin by tropomyosin.


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