Isolation and characterization of a low molecular weight chondroitin sulfate proteoglycan from rabbit skeletal muscle

Biochemistry ◽  
1987 ◽  
Vol 26 (11) ◽  
pp. 3149-3156 ◽  
Author(s):  
Narayanan Parthasarathy ◽  
Marvin L. Tanzer
1975 ◽  
Author(s):  
D. S. Pepper ◽  
S. Moore ◽  
J. D. Cash

The thrombin released products from washed human platelets were separated by filtration on 4% agarose in 0.15 M NaCl. The high molecular weight PF4 complex was dissociated and re-chromatographed in 0.75 M NaCl. The low molecular weight fraction, including β thromboglobulin and a low MW anti-heparin was freed of plasminogen anti-activator by dissociation and chromatography in pH 3.5 pyridine acetic acid. The anti-activator was irreversibly denatured and albumin was removed in the void volume of the column. A more suitable purification procedure for recovery of all activities was affinity chromatography on heparin-agarose. The anti-activator was excluded and could be obtained free of plasma proteins by Sephadex G-200 chromatography. The βTG eluted at 0.3 M NaCl and the low MW anti-heparin at 1.5 M NaCl. The pure βTG (MW 36,000) was injected into rabbits and the resulting antiserum used to produce a radioimmunoassay for the release reaction in vivo.


Life Sciences ◽  
1987 ◽  
Vol 41 (3) ◽  
pp. 297-304 ◽  
Author(s):  
M.H. Heulin ◽  
J. Rajoelina ◽  
M. Artur ◽  
C. Geschier ◽  
J. Straczek ◽  
...  

1996 ◽  
Vol 5 (4) ◽  
pp. 445-451 ◽  
Author(s):  
Menelas N. Pangalos ◽  
Junichi Shioi ◽  
Spiros Efthimiopoulos ◽  
Anfan Wu ◽  
Nikolaos K. Robakis

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