In vitro inhibition of the classical pathway of human complement by a natural microbial product, colistin sulphate

1986 ◽  
Vol 35 (17) ◽  
pp. 2917-2921 ◽  
Author(s):  
Syed Shafi Asghar ◽  
Annemiek de Koster ◽  
Hayo J. van der Helm
Keyword(s):  
Classical Pathway ◽  
Human Complement ◽  
Microbial Product ◽  
In Vitro Inhibition

In vitro inhibition of the classical pathway of human complement by polymyxin B

1987 ◽  
Vol 36 (18) ◽  
pp. 2927-2930 ◽  
Author(s):  
Syed Shafi Asghar ◽  
Tom Boot ◽  
Hayo J. Van Der Helm
Keyword(s):  
Polymyxin B ◽  
Classical Pathway ◽  
Human Complement ◽  
In Vitro Inhibition

scholarly journals Soluble C3 proconvertase and convertase of the classical pathway of human complement. Conditions of stabilization in vitro

1985 ◽  
Vol 226 (2) ◽  
pp. 429-436 ◽  
Author(s):  
M B Villiers ◽  
N M Thielens ◽  
M G Colomb
Keyword(s):  
Density Gradient ◽  
Binding Protein ◽  
Sucrose Density Gradient ◽  
Density Gradient Ultracentrifugation ◽  
Classical Pathway ◽  
Human Complement ◽  
Proteolytic Fragment ◽  
The Individual

Soluble classical-pathway C3 convertase and proconvertase were prepared from purified C4b-C2ox complex in the presence of Ni2+; the two complexes, stable for at least 15 h at 4 degrees C, were isolated by sucrose-density-gradient ultracentrifugation. The C3 convertase alone was able to cleave C3, and its decay was accelerated in the presence of C4-binding protein. The individual roles of Ni2+ and I2 treatment of C2 in the stabilization of the complexes seemed to be different and additive. 63Ni2+ binding coupled to h.p.l.c. analysis showed that 63Ni2+ bound only to the C2ox proteolytic fragment a (1 mol/mol) with a Kd of 26 microM. Competition studies between Ni2+ and Mg2+ indicated that only half of the Ni2+ bound to the C3 convertase was removed by Mg2+, whereas, in the same conditions, Ni2+ bound to C2ox proteolytic fragment a was not displaced, suggesting the presence of two sets of sites on the convertase. EDTA prevented the formation of both C3 convertase and proconvertase; EDTA had no effect on the preformed C3 convertase, whereas it dissociated the preformed proconvertase.

Effekte von Substanz P und Neurotensin auf die Kontraktilität des Ileums der Maus in vitro: Inhibition durch STW 5

2007 ◽  
Vol 45 (08) ◽  
Author(s):  
D Hagelauer ◽  
O Kelber ◽  
D Weiser ◽  
S Laufer ◽  
H Heinle
Keyword(s):  
Substanz P ◽  
In Vitro Inhibition

In vitro Inhibition of Pancreatic Enzyme Activities by Dietary Fiber

Digestion ◽  
1982 ◽  
Vol 24 (1) ◽  
pp. 54-59 ◽  
Author(s):  
G. Isaksson ◽  
I. Lundquist ◽  
I. Ihse
Keyword(s):  
Dietary Fiber ◽  
Enzyme Activities ◽  
Pancreatic Enzyme ◽  
In Vitro Inhibition
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