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Proteins, cellular digestion

The body contains many amino acids, some of which can be synthesized (non-essential amino acids), while others must be absorbed from the diet (the essential amino acids). Amino acids are the building blocks of protein, being attached together in groups to form the proteins that the body needs as part of its cellular structure or as enzymes, which are biological catalysts. Glutamate can be synthesized in the body, and it is also absorbed from food, in which it occurs as the free amino acid, or it can be released from proteins by digestion. [Pg.279]

Dietary protein is digested in the intestine, producing amino acids that are transported throughout the body. Cellular proteins are degraded at widely variable rates, ranging from minutes to the life of the organism. [Pg.976]

The synthesized or synthetic proteins previously discussed in terms of the genetic code are not necessarily the same as those that start out as nutritional or dietary proteins. However, digestive enzymes break down dietary proteins into the amino acid pool required for subsequent cell protein synthesis, as has been described. The proteins so synthesized variously become cellular structural components, enzymes and hormones, and blood plasma proteins. The latter are involved in cellular osmotic balances, that is, in ensuring a stable pressure difference across the cell walls. These blood proteins also transport substances through the vascular system, and assist in promoting inununity (Chaney, in Devlin, 1986, p. 1179ff). [Pg.134]

Most often proteins are the bacterial biopolymers studied using MALDI MS either from fractions or whole cells. They are not the only isolated cellular biopolymers studied by MALDI, nor the first. Very soon after the introduction of MALDI there were a few reports of the analysis of bacterial RNA or DNA from bacterial fractions. One of the first applications of MALDI to bacteria fractions involved analysis of RNA isolated from E. coli,4 Other studies included analysis of PCR-amplified DNA,5 6 DNA related to repair mechanisms7 and posttranscriptional modification of bacterial RNA.8 While most MALDI studies involve the use of UV lasers, IR MALDI has been reported for the analysis of double stranded DNA from restriction enzyme digested DNA plasmids, also isolated from E. coli.9... [Pg.128]

A number of proteomic studies on archival material have utilized Liquid Tissue (Expression Pathology, Inc., Gaithersburg, MD), a commercial protein extraction kit for FFPE tissue.4,9,25-28 This kit is also based upon HIAR techniques and shares a similar work flow to the methods already discussed. Thin, typically 5-10pM, sections are cut from paraffin tissue blocks, the paraffin is removed, and the tissue deparaffinized and rehydrated in alcohols and distilled water before microdissection. The cellular material is then suspended in Liquid Tissue buffer and heated at 95°C for 90 min. Trypsin is added, and the material is digested overnight at 37°C prior to reduction with DTT and analysis by LC-MS/MS.26... [Pg.340]

Ricin is a potent cellular protein toxin contained in the beans of the castor been plant (Ricinus communis), which is extensively cultivated for oil production and is also a common ornamental garden plant. Ricin is able to inhibit ribosomal protein synthesis eventually causing cell death, and owing to these properties it has been allegedly used in terrorist and criminal activities. After trypsin digestion of castor bean crude extracts, Ostin et al. [105] were able to unambiguously... [Pg.672]


See other pages where Proteins, cellular digestion is mentioned: [Pg.40]    [Pg.289]    [Pg.71]    [Pg.273]    [Pg.405]    [Pg.165]    [Pg.520]    [Pg.1874]    [Pg.320]    [Pg.169]    [Pg.503]    [Pg.32]    [Pg.336]    [Pg.114]    [Pg.301]    [Pg.115]    [Pg.225]    [Pg.129]    [Pg.141]    [Pg.311]    [Pg.165]    [Pg.324]    [Pg.352]    [Pg.49]    [Pg.147]    [Pg.389]    [Pg.195]    [Pg.538]    [Pg.375]    [Pg.386]    [Pg.130]    [Pg.251]    [Pg.155]    [Pg.228]    [Pg.215]    [Pg.214]    [Pg.177]    [Pg.392]    [Pg.408]    [Pg.503]    [Pg.383]    [Pg.195]    [Pg.538]   
See also in sourсe #XX -- [ Pg.134 , Pg.136 , Pg.137 ]




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Protein digestibility

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