By C B Anfinsen
ADVANCES IN PROTEIN CHEMISTRY VOL 4.
Read Online or Download Advances in Protein Chemistry, 4 PDF
Similar clinical chemistry books
This trip throughout the interesting global of molecular topology specializes in catenanes, rotaxanes and knots, their synthesis, homes, and functions and the idea of interlocking and interpenetrating molecules. approximately 100 years of development have handed considering that Willstatter's speculative imaginative and prescient of a molecule which include interlinked jewelry.
Each pupil can reap the benefits of additional aid with concerns of association and elegance within the writing of time period papers, theses, and dissertations - as a precursor to raised grades and larger admire. this useful advisor from the best-selling writer crew of "The artwork of clinical Writing" indicates the way to in achieving greatest gain with rather little attempt.
Delivering an updated assessment of the sphere, this reference offers vast discussions on a variety of ways for molecular imprinting written via pioneering specialists at the topic. Molecularly Imprinted fabrics: technological know-how and know-how deals experimental protocols that exemplify particular concepts, in addition to distinct surveys on molecular imprinting learn and functions.
- Plasma source mass spectrometry : the new millennium
- Gas Chromatography and Mass Spectrometry
- The chemistry of dienes and polyenes,vol. 2
- Comprehensive Microsystems
Additional resources for Advances in Protein Chemistry, 4
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.
Advances in Protein Chemistry, 4 by C B Anfinsen