Protein assessment

Hamdan, M.H., and Righetti, P.G. (2005) Proteomics Today Protein Assessment and Biomarkers Using Mass Spectrometry, 2D Electrophoresis, and Microarray Technology (Wiley-lnterscience Series on Mass Spectrometry), Wiley-lnterscience, ISBN-13 978-0471648178. 

Characterization of Purified Proteins Assessing purity, 182, 555 determining size, molecular weight, and presence of subunits, 182, 566 amino acid analysis, 182, 587 limited N-terminal sequence analysis, 182, 602 peptide mapping, 182, 613 analysis for protein modifications and nonprotein cofactors, 182, 626 protein crystallization, 182, 646. 

Methods for assessing protein purity must quantitate the amount of target protein relative to the amount of contaminant(s) in the sample. This requires two separate analytical methods one for the taiget protein and one for the total protein including contaminants. For example, with enzymatic proteins, assessment of functional purity typically relies on kinetic assays in which the amount of substrate consumed or product produced per unit time is proportional to the amount of enzyme present. The total activity of the sample is calculated and compared to the total amount of protein to give the specific activity of the sample. Methods for determining total protein are discussed in Chapter Bl. An increase in specific activity at a purification step reflects a loss of contaminant proteins. 

Fujiyama, A., Matsumoto, K., and Tamanoi, F. (1987). A novel yeast mutant defective in the processing of ras proteins assessment of the effect of the mutation on processing steps. EMBO J 6 223-228. 

Bangham, D.R. (1988). Control of new biologicals in the United Kingdom personal view from a biologist. In Therapeutic Peptides and Proteins Assessing the New Technologies. D.R.Marshak and D.T.Liu, eds. (New York Cold Spring Harbor Laboratory), pp. 279 292. 

Protein Assessment and Biomarkers Using Mass Spectrometry, 2D Electrophoresis, and Microarray Technology... 

B. Tams, J. E. Straub, and D. Thirumalai, Probing the initial stage of aggregation of the ApiO-35-protein assessing the propensity for peptide dimerizatio. J. Mol. Biol., 345... 

R95 P. Bemado and D. I. Svergun, Structural Insights into Intrinsically Disordered Proteins by Small-Angle X-Ray Scattering , in Instrumental Analysis of Intrinsically Disordered Proteins Assessing Structure and Conformation eds. V. Uversky and S. Longhi, John Wiley Sons, Inc., Hoboken, N. J., 2010, p. 451. 

For scientists studying the effects of process-induced changes in food proteins, assessment of denaturation has frequently been based on the one hand by a measured loss of solubility, i.e., the functional definition of denaturation, and on the other hand, by changes from the native structure using techniques requiring non-turbid solutions of proteins at low concentrations. Neither of these criteria is completely satisfactory for food systems in which proteins may be present at high concentrations, and in which solubility or loss thereof may not be directly related to other functional properties of interest. In fact, many foods are not solutions. 

Assessment of synthetic function serum ALAT, ASAT, ornithine carbamyl transferase, albumin globulin, coagulation profile, prothrombin time, partial thromboplastin time, radioactive amino acids, electrophoresis techniques for serum proteins Assessment of excretion function gamma-glutyml transferase, LDH, bilirubin, alkaline phosphatase... 

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