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Human globin

Lapolla A, Ragazzi E, Andretta B, et al. Multivariate analysis of matrix-assisted laser desorption/ionization mass spectrometric data related to glycoxidation products of human globins in nephropathic patients. J. Am. Soc. Mass. Spectrom. 2007 18 1018-1023. [Pg.389]

Karlsson, S., and A. W. Nienhius, Developmental regulation of human globin genes. Ann. Rev. Biochem. 54 1071-1108, 1985. [Pg.827]

Fig. 5. The switch in human globin chain synthesis at birth. Fig. 5. The switch in human globin chain synthesis at birth.
Products Formed on Chynwtryptic Hydrolysis of ce-Chatns of Human Globin under Two Different Conditions of Hydrolysis ... [Pg.73]

In 12 workers who were occupationally exposed to ethylene oxide during the sterilization of medical equipment, concentrations of 0.2-8.5 ppm were detected (2). This study also confirmed the relation between the ethylene oxide concentration in ambient air and the amount of A-2-hydroxyethylvaline in human globin, which has been used as a biological marker of carcinogenicity. [Pg.1297]

Fig. 1. HPLC of tryptic digest of human globins (a and P)from hemoglobin treated in vitro with [8-14C] styrene-7,8-oxide (a) chromatogram numbers refer to fractions, (b) radiogram annotation refers to tryptic peptide. Fig. 1. HPLC of tryptic digest of human globins (a and P)from hemoglobin treated in vitro with [8-14C] styrene-7,8-oxide (a) chromatogram numbers refer to fractions, (b) radiogram annotation refers to tryptic peptide.
Table 1. Tryptic peptides from human globins (a and P) identified by liquid secondary ion mass spectrometry after C-18 reversed phase HPLC fractionation... Table 1. Tryptic peptides from human globins (a and P) identified by liquid secondary ion mass spectrometry after C-18 reversed phase HPLC fractionation...
Changes in human globin chain concentration during development. [Reproduced with permission from W. G. Wood, Hemoglobin synthesis during human fetal development. Br. Med. Bull. 32, 282 (1976).]... [Pg.658]

Figure 7.22 Expression of human globin genes at different stages of development. [Pg.1920]

A number of other colloids have also been used or proposed as potential expanders, but have not found clinical application because of various types of severe adverse reactions. One example is Alginon which is prepared by polymerization of sodium alginate (Tomoda and Inokuchi 1959). Further, the following colloids have been studied (Thompson 1960) methylcellulose, pectin, hemoglobin, modified human globin, isinglass, bovine serum albumin, polyvinyl alcohol, and starch. [Pg.582]

Goodman M, Moore GW, Barnabas J, Matsuda G (1974) The phylogeny of human globin genes investigated by the maximum parsimony method. J Mol Evol 3 1-48... [Pg.65]

Inoue H, Maeno Y, Iwasa M, et al. (1997) Sensitive detection of human globin chains by microbore high-performance liquid chromatography and its forensic applications. Journal of Chromatography B, Biomedical Sciences Applications 688 221-227. [Pg.1633]

FIGURE 3 Fluorescence images of NRK cells with rhodamine-labeled actin microinjected into the cytoplasm (a) and with rhodamine-labeled human globin pre-messenger RNA microinjected into the nucleus (b). In (a), fluorescent actin becomes incorporated into cytoplasmic structures, with the nucleus appearing as a dark area. In (b), fluorescent pre-mRNA is localized almost exclusively inside the nucleus at numerous discrete sites. Nucleoli appear as dark patches. [Pg.20]

Nie, Z., Liu, Q., Xie, J., 2011. Improvements in monitoring the N-terminal valine adduct in human globin after exposure to sulfur mustard and synthesis of reference chemicals. Talanta 85, 1154-1159. [Pg.854]


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