Microspheres, human serum

Fig. 10 Release of cromolyn sodium (sodium cromoglycate) from human serum albumin microspheres prepared using a water-oil emulsion technique with 5% glutaraldehyde as cross-linking agent. Dissolution medium pH 7 phosphate buffer. (From Ref. 98.)... 

Zolle I, Hosein F, Rhodes BATK, Wagner HN Jr (1970) Human serum albumin microspheres for studies of the reticuloendothelial system. J Nucl Med 11 379. 

Tanaka E, Terada M, Misawa S, Wakasugi C. 1998. Erratum to Simultaneous determination of twelve benzodiazepines in human serum using a new reversed-phase chromatographic column on a 2um porous microspherical silica gel. J Chromatogr B Biomed Appl 709(2) 324. [J Chromatogr B 682 (1996) 173]. 

Tomlinson, E., Burger, J., and Schoonderwoerd, E. Human serum albumin microspheres for intraarterial drug targeting of cytostatic compounds, pharmaceutical aspects and release characteristics, in Microspheres and Drug Therapy. Pharmaceutical, Immunological and Medical Aspects, ed. S. Davies et al. New York Elsevier Science Publishers, 1984, pp. 217-227. 

More recently 211 At adsorbed on silver coated human serum albumin (HSA) microspheres has been used by Wunderlich, Doberenz and their colleagues46,94-99 to study the accumulation of the isotope in some tumour-bearing tissues of mice and pigs, and in one special case for human therapy100. 

Li, X., Deng, X., and Huang, Z. (2001), In vitro protein release and degradation of poly-DL-lactide-poly(ethylene glycol) microspheres with entrapped human serum albumin Quantitative evaluation of the factors involved in protein release phase, Pharm. Res., 18,117-124. 

Coupling reactions of various proteins to the cellulose microspheres can be conducted by the CNBr activation method [29]. The proteins employed are bovine serum albumin (BSA), bovine immunoglobulin G(IgG), gelatin, tuftsin, and human serum fibronection (FN). 

Hora MS, Rana RK, Nunberg JH, Tice TR, Gilley RM, Hudson ME. Release of human serum albumin from poly(lactide-co-glycolide) microspheres. Pharm Res 1990 7 1190-1194. 

Zolle I, Kropf G (1982) Factors affecting the trapping and clearance of microspheres. In Anghilieri L (ed) General processes of radiotracer localization, vol. 2. CRC Press, Boca Raton, pp 15-38 Zolle I, Rhodes BA, Wagner HN Jr (1970) Preparation of metabolizable radioactive human serum albumin microspheres for studies of the circulation. Int J Appl Rad Isot 21 155-167... 

Ga-protelns can be formed and that the labeled protein is stable for a time period of several hours. The same type of linkage has also been used to attach galllum-68 to human serum microspheres (51). 

In the measurement of pulmonary perfusion, Ga-labeled albumin microspheres have been used extensively [79]. Pulmonary perfusion involves vascular injection of labeled microspheres sized such that they will be mechanically trapped by the first capillary bed they encounter [80]. Previously, a commercial albumin microsphere kit (3M Instant Microspheres) was used in the preparation of Ga microspheres however, this product has been discontinued. Methods were developed to radiolabel macroaggregated human serum albumin (HSA) with Ga using a lyophilized Technescan MAA kit (Mallinckrodt Inc.) [25,33]. 

A number of additional examples of protein delivery via polysaccharides are available in the scientific and patent literature. Edman et al. (1980) have demonstrated release of carbonic anhydrase, catalase, human serum albumin, and immunoglobulin G from cross-linked biodegradable polyacryl dextrans having molecular weights ranging from 10,000 to 2,000,000. Thermal stability of carbonic anhydrase was found to be enhanced via entrapment in microspheres of the above polymer. Schroder (1984) has shown that... 

He J, Feng M, Zhou X, Ma S, Jiang Y, Wang Y, Zhang H. Stabihzation and encapsulation of recombinant human erythropoietin into PLGA microspheres using human serum albumin as a stabilizer. Int J Pharm. 416 (1) 69-76, 2011. 

The usefulness of the third strategy, based on adsorption of bioactive compounds onto the surface of microspheres, was verified for preparation of poly(D,L-lactide) and PCL microspheres with adsorbed proteins. The protein-loaded particles were obtained by incubation of poly(D,L-lactide) (Dn = 2.50 J.m) or PCL (Dn= 0.63 pm) microspheres with human semm albumin or with human y-globulin solutions. PCL microspheres with the maximal content of human semm albumin and y-globulin equal to 9.0% and 23.6% (w/w), respectively, were obtained. In the case of much larger poly(D,L-lactide) microspheres, the maximal protein content was equal to 2.1% and 4.0% for human serum albumin and y-globulin, respectively. 

Dolitzky, Y., Sturchak, S., Nizan, B., Sela, B.A., and Margel, S. (1994). Synthesis, characterization, and use of immobilized polyacrolein microspheres in diagnostics—a model determination of alpha) 1 )-antitrypsin in human serum. Analyt. Biochem. 220 (2), 257-267. 

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