Human serum albumin label

Cheung D, Bowen B, Rashid F, Rhem R, Dolovich M. Preparation of microaggre-gated human serum albumin labelled with Tc to enable in vivo evaluation of suspension aerosols. Am J Resp Crit Care Med 1998 157 A638. 

Scheme 8.20 Synthesis of human serum albumin labeled with a rhenium tricarbonyl fragment.

Catalase has also been used as an enzyme label in competitive heterogeneous enzyme immunoassays. Catalase generates oxygen from hydrogen peroxide with the oxygen determined amperometrically with an oxygen electrode. This approach has been demonstrated for a-fetoprotein theophylline and human serum albumin... 

The syntheses, photophysical and electrochemical properties of [Ir(ppy)2(phen-NS-5)]PF6, (181), [Ir(ppy)2(phen-NHCOCH2I-5)]PF6, (182), and [Ir(ppy)2(phen-NH2-5)]PF6 are reported.342 Complexes (181) and (182) have been used to label amine- and sulfhydryl-modified oligonucleotides and human serum albumin to give luminescent bioconjugates. 

J.D. Jordan, R.A. Dunbar, and F.V. Briht, Dynamics of scrylodan-labeled bovine and human serum albumin entrapped in a sol-gel-derived biogel. Anal. Chem. 67, 2436—2443 (1995). 

Several methods for measuring drug binding to human serum albumin involving the determination of retention times on HPLC columns with bound albumin have been reported [77,78]. Solid-phase microextraction [79,80], capillary electrophoresis [81], and displacement of near-infrared fluorescent labels [82] have all been studied. 

Figure 12.6. Fluorescein-labelled aconylated human serum albumin distribution in the cross-section of a rat liver slice ( 250 jrM) after 120 min incubation. Bar = 100 [xM.

Fig. 3 Electropherograms illustrating the competitive binding of ketoprofen and quinidine to noncovalently dye-labeled human serum albumin. 100 nM heptamethine cyanine dye and (A) 50 nM human serum albumin, (B) 50 nM human serum albumin, 50 nM quinidine, (C) 50 nM human serum albumin, 50 nM ketoprofen. (Reprinted with permission from Ref. 47. Copyright 2001 Wiley-VCH.)...

ED Moody, PJ Viskari, CL Colyer. Noncovalent labeling of human serum albumin with indocyanine green a study by capillary electrophoresis with diode laser-induced fluorescence detection. J Chromatogr B 729 55-64, 1999. 

In addition to the application of roughened Ag electrodes in SERS measurements, one should add that Geddes et al. [15] have described the use of such Ag electrodes in metal-enhanced fluorescence studies also. The constant current flowing between two silver electrodes in pure water facilitated the growth of fractal-like structures on the cathode. The electrode was coated with a monolayer of human serum albumin protein labeled with Indocyanine Green. It was observed that the fluorescence intensity on the roughened electrode increased approximately the 50-fold, compared to the unroughened electrode. 

Instead of using human serum albumin as a carrier protein, other workers (135) utilized ovalbumin for preparing the diazotized clenbuterol antigen in an enzyme immunoassay developed for screening of clenbuterol residues in bovine urine, liver, and eye. Alkaline phosphatase rather than -galactosidase was also used as an enzyme label in the preparation of the enzyme-clenbuterol conjugate. 

Heineman s group [13,14] proposed the method of heterogeneous immunoassay to detect human serum albumin (HSA) labeled with In... 

On these bases, proteins like human serum albumin (HSA) and avidin (Av) have been labelled with such complexes. This yields bioconjugates that are strongly luminescent and can be used for recognition purposes [79]. In Table 10 are listed luminescence properties of some selected complexes and related bioconjugates [79]. 

II. Ikariyama, Y., Suzuki, S., andAizawa, M., Luminescence immunoassay of human serum albumin with hemin as labeling catalyst. Anal. Chem. 54, 1126-1129 (1982). 

Figure 3.18. Data on the correlation frequency of the mobility of physical labels and their environment in bovine and human serum albumins and in the photosynthetic RC (I) and the rate constants of ET s primary donor (P) to the bacteriaophephytin acceptor (II) in the Arrhenius coordinates. (Likhtenshein, 1996). Reproduced with permission.

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