scholarly journals 3-O-methyl sugars as constituents of glycoproteins. Identification of 3-O-methylgalactose and 3-O-methylmannose in pulmonate gastropod haemocyanins

1977 ◽  
Vol 165 (1) ◽  
pp. 173-176 ◽  
Author(s):  
R L Hall ◽  
E J Wood ◽  
J P Kamberling ◽  
G J Gerwig ◽  
F G Vliegenthart

In addition to the already knownonosaccharides fucose, xylose, mannose, galactose, glucose, N-acetylgalactosamine and N-acetylglucosamine, the carbohydrate part of the haemocyanin from Helix pomatia (Roman snail) contains 3-O-methylgalactose, and that from Lymnaea stagnalis (a freshwater snail) 3-O-methylgalactose and 3-O-methylmannose. The 3-O-methyl sugars were identified by g.l.c.-mas spectrometry of the corresponding trimethylsilyl methyl glycosides and the alditol acetates, and by co-chromatography with the synthetic reference substances.

Evolution ◽  
2004 ◽  
Vol 58 (12) ◽  
pp. 2747 ◽  
Author(s):  
Mikael Puurtinen ◽  
Mirjami Hytönen ◽  
K. Emily Knott ◽  
Jouni Taskinen ◽  
Kari Nissinen ◽  
...  

2014 ◽  
Vol 189 ◽  
pp. 87-91 ◽  
Author(s):  
Ana López-Serrano Oliver ◽  
Marie-Noële Croteau ◽  
Tasha L. Stoiber ◽  
Mila Tejamaya ◽  
Isabella Römer ◽  
...  

1979 ◽  
Vol 196 (3) ◽  
pp. 545-548 ◽  
Author(s):  
T. Sminia ◽  
W. P. W. van der Knaap ◽  
F. G. M. Kroese

1999 ◽  
Vol 114 (4) ◽  
pp. 535-550 ◽  
Author(s):  
Shalini Gera ◽  
Lou Byerly

Ca2+ channel inactivation in the neurons of the freshwater snail, Lymnaea stagnalis, was studied using patch-clamp techniques. In the presence of a high concentration of intracellular Ca2+ buffer (5 mM EGTA), the inactivation of these Ca2+ channels is entirely voltage dependent; it is not influenced by the identity of the permeant divalent ions or the amount of extracellular Ca2+ influx, or reduced by higher levels of intracellular Ca2+ buffering. Inactivation measured under these conditions, despite being independent of Ca2+ influx, has a bell-shaped voltage dependence, which has often been considered a hallmark of Ca2+-dependent inactivation. Ca2+-dependent inactivation does occur in Lymnaea neurons, when the concentration of the intracellular Ca2+ buffer is lowered to 0.1 mM EGTA. However, the magnitude of Ca2+-dependent inactivation does not increase linearly with Ca2+ influx, but saturates for relatively small amounts of Ca2+ influx. Recovery from inactivation at negative potentials is biexponential and has the same time constants in the presence of different intracellular concentrations of EGTA. However, the amplitude of the slow component is selectively enhanced by a decrease in intracellular EGTA, thus slowing the overall rate of recovery. The ability of 5 mM EGTA to completely suppress Ca2+-dependent inactivation suggests that the Ca2+ binding site is at some distance from the channel protein itself. No evidence was found of a role for serine/threonine phosphorylation in Ca2+ channel inactivation. Cytochalasin B, a microfilament disrupter, was found to greatly enhance the amount of Ca2+ channel inactivation, but the involvement of actin filaments in this effect of cytochalasin B on Ca2+ channel inactivation could not be verified using other pharmacological compounds. Thus, the mechanism of Ca2+-dependent inactivation in these neurons remains unknown, but appears to differ from those proposed for mammalian L-type Ca2+ channels.


2009 ◽  
Vol 157 (7) ◽  
pp. 2142-2146 ◽  
Author(s):  
Rachel C. Walton ◽  
Catherine R. McCrohan ◽  
Francis R. Livens ◽  
Keith N. White

Author(s):  
Theodorus C.M. Wijsman ◽  
Janneke J. Maaskant ◽  
Paul Balm ◽  
Job Klijnstra

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