scholarly journals THE CONVERSION OF FIBRINOGEN TO FIBRIN

1953 ◽  
Vol 36 (6) ◽  
pp. 759-766 ◽  
Author(s):  
Sidney Shulman ◽  
Sidney Katz ◽  
John D. Ferry

1. Fibrin clots prepared in the absence of calcium can be dissolved in solutions of lithium chloride and bromide and sodium bromide and iodide, as well as of guanidine hydrochloride and urea. These salts do not denature fibrinogen under the same conditions of concentration, temperature, and time. Sedimentation experiments on the fibrin solutions show in each case a single sharp peak with a sedimentation constant close to that of fibrinogen. 2. At lower concentrations, these salts inhibit the clotting of fibrinogen by thrombin, but in the case of lithium bromide and sodium iodide, at least, allow an intermediate polymer to accumulate whose sedimentation constant is close to that of the polymer observed in systems inhibited by hexamethylene glycol or urea.

1970 ◽  
Vol 46 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Yutaka Tashiro ◽  
Eiichi Otsuki

Ultracentrifugal analyses of the native silk proteins extracted from the various parts of the middle silk gland of the mature silkworm have revealed that there exist four components with S°20,w values of 10S, 9–10S, 9S, and 4S in the extract. It is suggested that the fastest 10S component is the native fibroin synthesized in the posterior silk gland and transferred to the middle silk gland to be stored there, while the slower three components probably correspond to inner, middle, and outer sericins which were synthesized in the posterior, middle, and anterior portion of the middle silk gland, respectively. Native fibroin solution was prepared from the most posterior part of the middle silk gland. Ultracentrifugal analyses have shown that the solution contains considerable amounts of aggregates in addition to the main 10S component. Treatment with lithium bromide (LiBr), urea, or guanidine hydrochloride solution up to 6 M all have failed to dissociate the 10S component. From the sedimentation equilibrium analyses and partial specific volume of 0.716, the molecular weight of the 10S component of the native fibroin solution was found to be between 3.2 – 4.2 x 105, with a tendency to lie fairly close to 3.7 x 105.


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