Beta-trace protein

Mclssac and Joshl, M. S. "Prenatal Detection of Neural Tube Defects. Comparison Between Alpha Fetoprotein and Beta-Trace Protein Assays". Amer. J. Obstet. Gynecol,... 

Giessing, M. (1999). Beta-trace protein as indicator of glomerular filtration rate. 

Hiraoka, A., et al (1998). Sodium dodecyl sulfate-capillary gel electrophoretic analysis of molecular mass microheterogeneity of beta-trace protein in cerebrospinal fluid from patients with central nervous system diseases./. Chromatogr. A 802, 143-8. 

Hiraoka, A., et al (2001). Charge microheterogeneity of the beta-trace proteins... 

Hoffmann, A., et al. (1993). Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid its identification as prostaglandin D synthase. J. Neurochem. 61, 451-6. 

Priem, F., et al. (1999). Beta-trace protein in serum a new marker of glomerular filtration rate in the creatinine-blind range. Clin. Chem. 45, 567-8. 

Tumani, H., et al. (1998). Beta-trace protein in cerebrospinal fluid a blood-CSF barrier-related evaluation in neurological diseases. Ann. Neurol. 44, 882-9. 

Blodom B, Mader M, Urade Y, Hayaishi O, Felgenhauer K, Bruck W. Choroid plexus the major site of mRNA expression for the beta-trace protein (prostaglandin D synthase) in human brain. Neurosci Lett 1996 209 117-120. 

Grabenhorst E, Hoffmann A, Nimtz M, Zettlmeissl G, Conradl HS. Construction of stable BHK-21 cells coexpressing human secretory glycoproteins and human Gal(beta l-4)GlcNAc-R alpha 2,6-sialyltransferase alpha 2,6-linked NeuAc is preferentially attached to the Gal(beta l-4)GlcNAc beta l-2)Man(aIpha l-3)-branch of diantennary oligosaccharides from secreted recombinant beta-trace protein. Eur. J. Biochem. 1995 232 718-725. 

E. Grabenhorst, M. Nimtz, J. Costa, H. S. Conradt, In vivo specificity of human alphal,3/4-fucosyltransferases III-VII in the biosynthesis of LewisX and sialyl LewisX motifs on complex-type N- glycans. Coexpression studies from Bhk-21 cells together with human beta-trace protein, J Biol Chem, (1998), 273, 30985-94. 

Hora et al. [3.19] described the complexity of protein stabilization by the example of recombinant, human Interleukin-2 (rhIL-2). Formulations with amino acids and mannitol/ sucrose are sensitive to mechanical stress e. g. by pumping. Hydroxypropyl-beta-cyclodextrin (HPcD) provides stability, but increases the sensitivity to oxygen. Polysor-bate 80 forms a mechanically stable product, but results in oxidation. In both cases contamination in the HPcD or traces of H202 in the Polysorbate may have been the starter for the oxidation. Brewster [3.20] reports, that HPcD stabilizes interleukin without forming aggregations and this results in 100 % biopotency. 

Fig. 6. Deconvolved amide F region FTIR spectra of apo- and heme-hemopexin. The amide F FTIR spectra of apo- and heme-hemopexin in D2 O were recorded and curve-fitted to resolve the individual bands. The differences between the original and fitted curves are shown in the upper traces in the panels. The estimated helix (15%), beta (54%), turn (19%), and coil (12%) content of the apo-protein are not significantly changed upon heme binding 104). This analysis was required because of the positive 231-nm elhpticity band in hemopexin and is consistent with the derived crystal structure results.

The vibrational spectra of reference material are introduced in Figure 3.1, which belong to the main components of soft tissue. The IR spectrum (trace A) and Raman spectrum (F) of the all-beta protein concanavalin A are shown in Figure 3.1. IR bands due to the peptide backbone with P-sheet secondary structures are found at 3284 (amide A), 1636 (amide I), 1531 (amide II), and 1235 cm-i (amide III). Bands at 1403 (COO ) and 2963, 2874, 1455 cm- (CHg) are assigned to amino acid side chains. These bands are located in the Raman spectrum at similar positions at 1398 and 1449 cm . The Raman amide I band is centered at 1672 cm , the amide III band at 1238 cm , and the weak amide II band is not observed. Instead, other Raman bands of amino acids are identified at 759 and 1555 cm for Trp 621,1003, 1031, and 1208 cm for Phe 643, 829, and 853 cm for Tyr and 1126, 1317, and 1340 cm (CH2/CH3) for aliphatic amino acids. The IR spectrum (B) and Raman spectrum (G) of the all alpha protein bovine serum albumin show a number of differences. The amide bands... 

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