Download PDF by C B Anfinsen: Advances in Protein Chemistry, 4

By C B Anfinsen

ISBN-10: 0080581773

ISBN-13: 9780080581774

ISBN-10: 0120342049

ISBN-13: 9780120342044

ADVANCES IN PROTEIN CHEMISTRY VOL 4.

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C. Heat of Melting. A careful investigation of the heat of melting of gelatin was made by Holleman, Bungenberg de Jong, and Modderman (1934). An isothermal determination is not possible, because the heat is absorbed over a considerable temperature range, as is readily seen from temperature-time curves (Lottermoser and Matthaes, 1929). Accordingly, an indirect method was employed. 6 g. per g. protein. These partially swollen gels were then introduced into a calorimeter and allowed to imbibe water to equilibrium.

The amino acid composition of fibrinogen is characterized by rather high proportions of residues containing sulfur and also hydroxyl groups (Brand, 1944, 1946). On the basis of a molecular weight of 500,000, the number of residues per molecule of human fibrinogen is: 113 of cysteine and half-cystine, 85 of methionine, 395 of serine, 277 of threonine, and 52 JOHN D. FERRY 160 of tyrosine. fibrin. Similar figures have been found for human and bovine 2. , the fibrinogen is converted to fibrin-by adding a small amount of another protein, thrombin, which also occurs normally in blood plasma in the form of an inactive precursor (prothrombin).

Dependence of Rigidity on Added Reagents. Substances which lower the melting points of gelatin gels also diminish M, x lo-' the rigidity a t a given temperature. 12. /liter. 0,5";@, 10";0 , 15". 2 by 2 M sodium bromide or so- Data of Ferry (1948). dium nitrate. 5 M and then increased. In the presence of potassium chloride, nitrate, or iodide, a steady decrease of elasticity with increasing salt concentration was observed, the magnitude of the effect increasing in the order named. 36 of the value in the absence of salt.

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Advances in Protein Chemistry, 4 by C B Anfinsen


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