scholarly journals A Freshwater Streptomyces, Isolated from Tyume River, Produces a Predominantly Extracellular Glycoprotein Bioflocculant

2012 ◽  
Vol 13 (7) ◽  
pp. 8679-8695 ◽  
Author(s):  
Uchechukwu U. Nwodo ◽  
Mayowa O. Agunbiade ◽  
Ezekiel Green ◽  
Leonard V. Mabinya ◽  
Anthony I. Okoh
Author(s):  
P. Hernández-Jáuregui ◽  
A. Sosa ◽  
A. González Angulo

Glycocalyx is the name given by Bennett to the extracellular glycoprotein coat present in some cell surfaces. It appears to play an important role in cell properties such as antigenicity, cell adhesivity, specific permeability, and ATP ase activity. In the sperm this coat can be directly related to such important phenomena as capacitation and fertilization. The presence of glycocalyx in invertebrate spermatozoa has already been demonstrated. Recently Yanagimachi et al. has determined the negative charges on sperm surfaces of mammalian spermatozoa including man, using colloidal iron hydroxide. No mention was made however of the outer surface coat as composed of substances other than those confering a negative charge. The purpose of this work was therefore to determine the presence of a glycocalyx in human spermatozoa using alcian blue and lanthanum staining.


1994 ◽  
Vol 124 (10) ◽  
pp. 1891-1897 ◽  
Author(s):  
Raymond F. Burk ◽  
Kristina E. Hill

2009 ◽  
Vol 126 ◽  
pp. S287
Author(s):  
Stephen Martin ◽  
Varodom Charoensawan ◽  
Christian Soellner ◽  
Boris Adryan ◽  
Bernard Thisse ◽  
...  

1993 ◽  
Vol 113 (1) ◽  
pp. 77-80 ◽  
Author(s):  
Svetlana V. Kononova ◽  
Arnold B. Tsiomenko ◽  
Wladyslaw I. Golubev

2014 ◽  
Vol 463 (1) ◽  
pp. 93-102 ◽  
Author(s):  
Yoshinobu Kariya ◽  
Mayumi Kanno ◽  
Kana Matsumoto-Morita ◽  
Midori Konno ◽  
Yoshiki Yamaguchi ◽  
...  

Osteopontin is a multiphosphorylated extracellular glycoprotein that has important roles in various physiological and pathological phenomena. We demonstrate that osteopontin O-glycosylation affects its phosphorylation status, cell-spreading and -adhesion activities, and its association with β1 integrins.


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