Chemically cross-linked albumin microspheres for the controlled release of incorporated rose bengal after intramuscular injection into rabbits

Davis, S.S.; Mills, S. D.; Tomlinson, E.

doi:10.1016/0168-3659(87)90021-6

Cited by 14 publications

(6 citation statements)

References 15 publications

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“…External plasticization of the egg albumin coating was tried with propylene glycol and egg yolk (globulins and lecithin). In addition, a chemical crosslinking method (Widder et al 1982, Davis et al 1987 was also attempted for the denaturation of egg albumin, egg albumin + full yolk and egg albumin + half yolk (alglomix ?Emulsifying agent: a, 0 4 6 per cent w/v Span 80; b, 1 per cent w/v Span 80; c, Tween 20. $Dilution medium (DM): Po: phosphate buffer (pH 7-6), oAC, acetate buffer (pH4.8).…”

Section: Preparation Of Microspheresmentioning

confidence: 99%

“…Albumin has several properties which make it an attractive choice as a carrier (Tomlinson 1983, Poznansky andCleland 1980). The denaturation of albumin has been attained by heat coagulation (Deasy 1984, Ishizaka et al 1981, Ishizaka and Koishi 1983 and/or by treatment with formalin (Widder et al 1979(Widder et al ,1982, 2,3-butadione (Widder et al 1979,1982, Burger et al 1985 or glutaraldehyde (Burger et al 1985, Lee et al 1981, Davis et a/. 1987, Ratcliffe et al 1984.…”

Section: Introductionmentioning

confidence: 98%

“…1987, Ratcliffe et al 1984. T h e microspheres have been characterized by various physico-chemical parameters including density (Pal and Pal 1987), particle size distribution (Ishizaka and Koishi 1983), wall thickness (Si-Nang et al 1973, Pal andPal 1987), surface topography (Davis et al 1987, Longo et al 1982, Widder et al 1979, IR spectra and X-ray diffractograms (Pal and Pal 1987).…”

Section: Introductionmentioning

confidence: 99%

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Drug targeting using non-magnetic and magnetic albumin-globulin mix microspheres of mefenamic acid

Lalla¹,

Ahuja²

1991

Journal of Microencapsulation

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Optimum conditions for the preparation of non-magnetic and magnetic microspheres of albumin-globulin mix (alglomix) containing mefenamic acid have been standardized. The effect of various parameters has been investigated with regard to the appearance, yield, drug content and encapsulation efficiency. The physicochemical parameters of the microspheres such as density, particle size distribution, surface topography and wall thickness, as well as the magnetite contained within the magnetic microspheres, have been determined. The infrared spectroscopic analysis confirmed the encapsulation of the drug and absence of free drug on the surface of the microspheres. The X-ray diffraction analysis confirmed that the crystallinity of the drug remained unchanged indicating thereby that no complex formation had taken place between core and coat materials. The in vitro release profiles of the microspheres have been studied. An attempt has also been made to check the in vivo efficacy in rats.

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Section: Preparation Of Microspheresmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Drug targeting using non-magnetic and magnetic albumin-globulin mix microspheres of mefenamic acid

Lalla¹,

Ahuja²

1991

Journal of Microencapsulation

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“…In principle, natural polymers such as proteins, are metabolizable and can incorporate drugs or markers in a relatively non-specific fashion. Therefore, these macromolecules producing biodegradable particles whose physico-chemical properties can be modulated by the cross-linking methods employed for their production (Gupta et al, 1986;Davis et al, 1987). Furthermore, due to the presence of numerous functional groups (i.e.…”

Section: Introductionmentioning

confidence: 99%

Adaptive Immune Responses of Legumin Nanoparticles

Mirshahi

Irache²,

Nicolas

et al. 2002

Journal of Drug Targeting

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Legumin is one of the main storage proteins in the pea seeds (Pisum sativum L.) and the molecules of this protein have the capacity of binding together to form nanoparticles after aggregation and chemical cross-linkage with glutaraldehyde. The aim of this work was to study the adaptive immune response of legumin nanoparticles in rats. Following intradermal immunisation with the native protein legumin and legumin nanoparticles of about 250 nm, the humoral and cell-mediated immune responses were analysed in rats. The humoral responses against legumin and legumin nanoparticles were examined by western blot and ELISA analysis. Both techniques clearly showed that sera from rats immunised with legumin strongly expressed antibodies against this protein. On the contrary, serum samples from rats inoculated with legumin nanoparticles did not contain detectable amounts of antibodies. These results may be explained by a reduction on the antigenic epitopes of the protein induced by the glutaraldehyde used during the cross-linking step. Concerning the cell-mediated response, neither legumin nor legumin nanoparticles stimulated an immunogenic response. This absence of response of spleen lymphocytes for legumin and legumin nanoparticles may be explained by a cytostatic effect of legumin which was corroborated by the evaluation of the middle phase of cell apoptose. In fact, both legumin and legumin nanoparticles are potent inductors of a cytostatic phenomenon and showed a significant increase of the chromatin condensation (p < 0.05) as compared with control.

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“…peptides [6], steroids [7,8] and low molecular weight, water-soluble compounds [9 ] have been incorporated. Among the drugs incorporated, cyto-*Paper presented at the Fourth International Symposium on Recent Advances in Drug Delivery Systems, Salt Lake City, UT, U.S.A., February 21-24, 1989. static agents (i.e.…”

Section: Introductionmentioning

confidence: 99%