Isolation and characterization of proteolytic fragments of the sea urchin sperm receptor that retain species specificity

1986 ◽  
Vol 118 (1) ◽  
pp. 202-208 ◽  
Author(s):  
Norka Ruiz-Bravo ◽  
William J. Lennarz
1999 ◽  
Vol 258 (3) ◽  
pp. 616-623 ◽  
Author(s):  
Kaoru Ohta ◽  
Chihiro Sato ◽  
Tsukasa Matsuda ◽  
Masaru Toriyama ◽  
William J. Lennarz ◽  
...  

Toxicon ◽  
1965 ◽  
Vol 3 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Charles B. Alender ◽  
George A. Feigen ◽  
Joseph T. Tomita

1981 ◽  
Vol 195 (1) ◽  
pp. 171-176 ◽  
Author(s):  
V Giancotti ◽  
S Cosimi ◽  
P D Cary ◽  
C Crane-Robinson ◽  
G Geraci

The separation and purification of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis is described. Physical studies were used to compare this histone H1 molecule with H1 histones from other species. C.d. and 270 MHz n.m.r. spectroscopy indicate that, despite significant compositional differences from other sea-urchin sperm H1 histones, their secondary and tertiary structures are very similar. A large difference in helicity was, however, found between S. granularis histone H1 and calf thymus histone H1, and their n.m.r. and fluorescence spectra also differ considerably. It is concluded that secondary structure and tertiary structure have not been conserved in the evolution of the H1 histone family.


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