scholarly journals Lanthanoid complex of iron-transport protein, transferrin - Kinetic study on release of the metal from N and C binding sites.

1988 ◽  
pp. 452-458 ◽  
Author(s):  
Takaki YAMAMURA ◽  
Kaoru ICHIMURA ◽  
To'ru TSUDA ◽  
Atsuko HAYASHI ◽  
Takahiro TANIGUCHI ◽  
...  
Neonatology ◽  
1992 ◽  
Vol 61 (2) ◽  
pp. 82-91 ◽  
Author(s):  
Frank J. Michel ◽  
Maria Filomena V. Fliss ◽  
Fuller W. Bazer ◽  
Rosalia C.M. Simmen

1995 ◽  
Vol 50 (10) ◽  
pp. 1619-1625 ◽  
Author(s):  
Carlos Soria ◽  
Victoria Revilla ◽  
Maria Adoración Candelas ◽  
Pedro Calvo ◽  
Arsenio Fernández-López

Metallomics ◽  
2010 ◽  
Vol 2 (10) ◽  
pp. 683 ◽  
Author(s):  
Mechthild Grebe ◽  
Daniel Pröfrock ◽  
Antje Kakuschke ◽  
Jose A.C. Broekaert ◽  
Andreas Prange

2012 ◽  
Vol 90 (3) ◽  
pp. 245-251 ◽  
Author(s):  
Jeremy H. Brock

It is now some 50 years since iron-binding lactoferrin was first isolated and purified, an event that opened the way to subsequent extensive research on lactoferrin structure and function. The initial recognition that lactoferrin closely resembled the plasma iron-transport protein transferrin meant that lactoferrin was first thought to mediate intestinal iron absorption or to act as an antimicrobial agent. It was also suggested that it could mediate the hyposideraemia of inflammation. This paper will assess to what extent early proposals have stood the test of time and also suggest possible mechanisms by which lactoferrin can mediate the large number of potential functions that have subsequently been proposed. It will also review the ability of lactoferrin to resist digestion in the gastrointestinal tract and identify areas for future research.


Blood ◽  
1980 ◽  
Vol 55 (2) ◽  
pp. 240-242 ◽  
Author(s):  
GM Galbraith ◽  
RM Galbraith ◽  
A Temple ◽  
WP Faulk

Abstract It has been postulated that the transplacental passage of maternal iron to the developing fetus requires binding of maternal transferrin to the trophoblast. We have therefore examined the ability of the human placenta to bind transferrin in vitro. Transferrin was demonstrated on trophoblast of human chorionic villi by immunohistologic methods. Moreover, after removal of transferrin bound in vivo by treatment of tissue with chaotropic solution or phosphate-buffered saline, freshly added transferrin was shown to bind in vitro in the same characteristic distribution. These findings suggest that placental iron transport is initiated by uptake of maternal transferrin iron to specific trophoblast binding sites.


2017 ◽  
Vol 61 (10) ◽  
pp. 407-415 ◽  
Author(s):  
Jimena Alvarez Hayes ◽  
Juan Marcos Oviedo ◽  
Hugo Valdez ◽  
Juan Martín Laborde ◽  
Fabricio Maschi ◽  
...  

2012 ◽  
Vol 205 (7) ◽  
pp. 1043-1047 ◽  
Author(s):  
Meghan A. Baker ◽  
Douglas Wilson ◽  
Kristina Wallengren ◽  
Andreas Sandgren ◽  
Oleg Iartchouk ◽  
...  

1974 ◽  
Vol 139 (3) ◽  
pp. 499-508 ◽  
Author(s):  
Neil Macfarlane ◽  
Stanley Ainsworth

The paper reports a study of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by pig liver pyruvate kinase when activated by fructose diphosphate and K+. The experimental results are consistent with two non-sequential mechanisms in which the substrates and products of the reaction are phosphoenolpyruvate, ADP, Mg2+, pyruvate and MgATP. Pyruvate release occurs before ADP binding. Two Mg2+ ions are involved, though the two Mg2+-binding sites cannot be occupied simultaneously. An isomerized enzyme complex forms before release of MgATP. Values were determined for the Michaelis constants of the reaction. Apparent MgATP inhibition constants are also given.


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