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0 -Globulin structure

H15. Hammond, G. L., Smith, C. L., and Underhill, D. A., Molecular studies of corticosteroid binding globulin structure, biosynthesis, and function. J. Steroid Biochem. Mol. Biol. 40, 755-767 (1991). [Pg.117]

Olsson, C., Langton, M., Hermansson, A.-M. (2002). Dynamic measurements of p-lacto-globulin structures during aggregation, gel formation and gel break-up in mixed biopolymer systems. Food Hydrocolloids, 16, 477 188. [Pg.300]

F. Franek (ed.). Gamma Globulines, Structure and Biosynthesis, Academic Press, London, 1969. [Pg.164]

Nussenzweig, V., and Benacerraf, B. (1967). 3rd Nobel Symp. Gamma Globulins—Structure and Control of Biosynthesis, p. 233. Interscience, New York. [Pg.343]

This structure encoding method has been applied both for the classification of a data set comprising 31 corticosteroids, for which affinity data were available in the literature, binding to the corticosteroid-binding globulin (CBG) receptor, and for the simulation of infrared spectra [28, 29). [Pg.415]

Table 5.7 Theoretically predicted polypeptides from the trypsin digestion of S-lacto-globulin (/3LG) . Reprinted from J. Chromatogr., A, 763, Turula, V. E., Bishop, R. T., Ricker, R. D. and de Haseth, J. A., Complete structure elucidation of a globular protein by particle beam liquid chromatography-Fourier transform infrared spectrometry and electrospray liquid chromatography-mass spectrometry - Sequence and conformation of /3-lactoglobulin , 91-103, Copyright (1997), with permission from Elsevier Science... Table 5.7 Theoretically predicted polypeptides from the trypsin digestion of S-lacto-globulin (/3LG) . Reprinted from J. Chromatogr., A, 763, Turula, V. E., Bishop, R. T., Ricker, R. D. and de Haseth, J. A., Complete structure elucidation of a globular protein by particle beam liquid chromatography-Fourier transform infrared spectrometry and electrospray liquid chromatography-mass spectrometry - Sequence and conformation of /3-lactoglobulin , 91-103, Copyright (1997), with permission from Elsevier Science...
Two of the cytoskeletal components, the actin filaments and the microtubules have been studied with molecular rotors. The main component of the actin filaments is the actin protein, a 44 kD molecule found in two forms within the cell the monomeric globulin form (G-actin) and the filament form (F-actin). Actin binds with ATP to form the microfilaments that are responsible for cell shape and motility. The rate of polymerization from the monomeric form plays a vital role in cell movement and signaling. Actin filaments form the cortical mesh that is the basis of the cytoskeleton. The cytoskeleton has an active relationship with the plasma membrane. Functional proteins found in both structures... [Pg.297]

Since antibodies occur in the globulin fraction of serum one predicts that the investigation of the fine structure of serum mucoproteins will become a problem of urgent immunological significance. It is doubtful however whether the carbohydrate group of mucoproteins can influence their immunological specificity.1 ... [Pg.213]

The extracellular domain of RPTKs can be composed of different structural motifs. For instance, the EGFR extracellular domain contains two cysteine-rich regions. The PDGFR extracellular domain consists of five immuno-globulin-like repeats. Other domains found in the extracellular region of RPTKs include fibronectin III repeats,... [Pg.419]

IgG 10-12 (80%) Monomeric structure (y-globulin) secreted from B cells during secondary response binds complement can cross placenta... [Pg.539]

Studies of the secondary structure of cucurbitin have shown its conformational modes consist of 5% a-helical, 32% pleated sheet, and 62% unordered structures (48). These values are similar in distribution to those of oTFfer oilseed globulins (48). [Pg.258]


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See also in sourсe #XX -- [ Pg.15 ]




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