scholarly journals Purified Horseshoe Crab Factor G

1995 ◽  
Vol 270 (2) ◽  
pp. 892-897 ◽  
Author(s):  
Tatsushi Muta ◽  
Noriaki Seki ◽  
Yoshie Takaki ◽  
Ryuji Hashimoto ◽  
Toshio Oda ◽  
...  
Keyword(s):  
Horseshoe Crab ◽  
Factor G

scholarly journals Factor G Utilizes a Carbohydrate-Binding Cleft That Is Conserved between Horseshoe Crab and Bacteria for the Recognition of β-1,3-d-Glucans

2009 ◽  
Vol 183 (6) ◽  
pp. 3810-3818 ◽  
Author(s):  
Yuki Ueda ◽  
Shuhei Ohwada ◽  
Yoshito Abe ◽  
Toshio Shibata ◽  
Manabu Iijima ◽  
...  
Keyword(s):  
Horseshoe Crab ◽  
Carbohydrate Binding ◽  
Binding Cleft ◽  
Factor G

Horseshoe Crab Factor G: A New Heterodimeric Serine Protease Zymogen Sensitive to (1→3)-β-D-Glucan

1996 ◽  
pp. 79-85 ◽  
Author(s):  
Tatsushi Muta ◽  
Noriaki Seki ◽  
Yoshie Takaki ◽  
Ryuji Hashimoto ◽  
Toshio Oda ◽  
...  
Keyword(s):  
Serine Protease ◽  
Horseshoe Crab ◽  
Factor G

scholarly journals Duplicated Binding Sites for (1→3)-β-d-Glucan in the Horseshoe Crab Coagulation Factor G

2002 ◽  
Vol 277 (16) ◽  
pp. 14281-14287 ◽  
Author(s):  
Yoshie Takaki ◽  
Noriaki Seki ◽  
Shun-ichiro Kawabata ◽  
Sadaaki Iwanaga ◽  
Tatsushi Muta
Keyword(s):  
Binding Sites ◽  
Horseshoe Crab ◽  
Coagulation Factor ◽  
Factor G

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

In vivo antimicrobial assay of the PPO system using horseshoe crab as the model animal

2007 ◽  
Author(s):  
Naxin Jiang ◽  
Nguan Soon Tan ◽  
Bow Ho ◽  
Jeak Ling Ding
Keyword(s):  
Horseshoe Crab ◽  
Model Animal ◽  
Antimicrobial Assay
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