Table 1.

Relative heparin affinities of native and cleaved forms of plasma and recombinant antithrombins



NaCl concentration at peak protein elution, M
Antithrombin
Native
Cleaved
Plasma wild type   1.43 ± 0.01   0.43* 
r-wild-type HA glycoform   2.09*  0.67 ± 0.02  
r-K125M HA glycoform   1.62  0.29 ± 0.02  
r-K114M HA glycoform   0.29 ± 0.01   0.36 ± 0.01  
r-wild-type LA glycoform   1.38 ± 0.02   0.71 ± 0.05  
r-K114M LA glycoform
 
0.26 ± 0.01
 
0.33 ± 0.02
 


NaCl concentration at peak protein elution, M
Antithrombin
Native
Cleaved
Plasma wild type   1.43 ± 0.01   0.43* 
r-wild-type HA glycoform   2.09*  0.67 ± 0.02  
r-K125M HA glycoform   1.62  0.29 ± 0.02  
r-K114M HA glycoform   0.29 ± 0.01   0.36 ± 0.01  
r-wild-type LA glycoform   1.38 ± 0.02   0.71 ± 0.05  
r-K114M LA glycoform
 
0.26 ± 0.01
 
0.33 ± 0.02
 

Plasma and recombinant (r) antithrombins, including both low-heparin affinity (LA) and high-heparin affinity (HA) glycoforms of the latter, were chromatographed on heparin-agarose as detailed in “Materials and methods.” All antithrombin forms were chromatographed at least twice except where noted, and average values for the salt concentrations at which the protein peak was eluted are reported with errors representing the range of observed values.

*

Identical values were obtained in 2 chromatography runs.

Latent antithrombin was eluted from the column at a similar value of 0.40 ± 0.01 M NaCl.

Value from a single chromatography run due to limited amounts of the sample.

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