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Journal ArticleDOI

Stability and release of bovine serum albumin encapsulated within poly(d,l-lactide-co-glycolide) microparticles

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TLDR
In this paper, size exclusion chromatographic analysis of bovine serum albumin (BSA) encapsulated within microparticles revealed that the covalent aggregation of BSA significantly occurred during the encapsulation process and throughout a release study.
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This article is published in Journal of Controlled Release.The article was published on 1997-02-17. It has received 163 citations till now. The article focuses on the topics: Bovine serum albumin.

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Citations
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Nano/micro technologies for delivering macromolecular therapeutics using poly(D,L-lactide-co-glycolide) and its derivatives.

TL;DR: Important findings of the past decade on the encapsulation and release profiles of macromolecular therapeutics from PLGA and PLGA-based nano/microparticles are discussed critically in relation to nature and type of bioactive molecule, carrier polymer and experimental variables that influence the delivery of macrochemical therapeutics.
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Protein instability in poly(lactic-co-glycolic acid) microparticles.

TL;DR: The use of various stabilization approaches has rendered some success in increasing protein stability, but, still, full preservation of the native protein structure remains a major challenge in the formulation of protein-loaded PLGA microparticles.
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Microencapsulation techniques, factors influencing encapsulation efficiency

TL;DR: The present article provides a literature review of different microencapsulation techniques and different factors influencing the encapsulation efficiency of the micro Encapsulation technique.
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Control of encapsulation efficiency and initial burst in polymeric microparticle systems

TL;DR: A literature review of the formulation parameters that are known to influence encapsulation efficiency and initial burst in the emulsion-solvent evaporation/extraction method is provided.
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Formulation aspects of biodegradable polymeric microspheres for antigen delivery.

TL;DR: This review provides an applicable summary of different formulation routes for the purpose of producing safe, qualified and efficacious products of microencapsulated peptide and protein antigens.
References
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Journal ArticleDOI

Controlled Delivery Systems for Proteins Based on Poly(Lactic/Glycolic Acid) Microspheres

TL;DR: Stability studies showed that the encapsulation of an enzyme inside PLGA microspheres can protect them from activity loss, and in vitro release studies revealed that different release profiles and release rates can be achieved by simply modifying factors in the preparation procedure.
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The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content

TL;DR: The similarities in the behavior of the BPA and BMA non-mercaptalbumin monomer fractions are somewhat surprising since the presence of these non-Mercapt albumin fractions in plasma albumin has been shown to be due to mixed disulfide formation between mercaptalbumin and plasma cysteine and glutathione.
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Moisture-induced aggregation of lyophilized proteins in the solid state.

TL;DR: A model system has been elaborated and investigated to elucidate the mechanism of the moisture‐induced aggregation of albumin and it has been discovered to be due to an intermolecular S—S bond formation via the thiol‐disulfide interchange reaction.
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Preparation of porous and nonporous biodegradable polymeric hollow microspheres

TL;DR: In this article, a simple method to prepare various porous and nonporous hollow microspheres composed of poly( d,l -lactic-co-glycolic acid) using a water/oil/water (W/O/W) multiple emulsion solvent evaporation technique is described.
Journal ArticleDOI

Importance of in vitro experimental conditions on protein release kinetics, stability and polymer degradation in protein encapsulated poly (d,l-lactic acid-co-glycolic acid) microspheres

TL;DR: Two proteins, carbonic anhydrase and bovine serum albumin, have been encapsulated as model protein drugs within microspheres composed of relatively fast degrading poly(d,l-lactic acid-co-glycolic acid, 50/50) to investigate protein stability problems.
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