In vivo conjugation of nasal lavage proteins by hexahydrophthalic anhydride

Johannesson, Gunvor; Lindh, Christian; Nielsen, Jörn; Björk, Birgitta; Rosqvist, Seema; Jönsson, Bo

doi:10.1016/j.taap.2003.09.001

Cited by 10 publications

(14 citation statements)

References 43 publications

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“…Lactferrin has attracted attention in recent years because it is a protein that exhibits various defensive functions in the body including anti-carcinogenic and immunoregulating actions (Togias 2003;Johhannesson et al 2004). Oral administration of the protein fails to send it without losing its activity to the intestines where it shows the above mentioned actions.…”

Section: Resultsmentioning

confidence: 99%

Preparation of tiny biodegradable capsules using electrocapillary emulsification

Abe

Nakayama²,

Kondo³

et al. 2007

Journal of Microencapsulation

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Conditions for preparing tiny biodegradable capsules were examined using electrocapillary emulsification that allows one to prepare monodisperse emulsions with ease by applying a DC potential between oil and water phases without mechanical agitation. The results obtained showed that a 1 : 4 mixture of polysorbate 80 (TO-10), a hydrophilic non-ionic surfactant, and sorbitan monooleate (SO-10), an oleophilic surfactant, is appropriate as the surfactant to be added to oil phase, cyclohexane is acceptable as the oil phase and 1000 V is optimum as the DC potential to be applied. The capsules prepared had sizes ranging from 100-300 nm and a surface roughness of approximately 10 nm and degraded in model intestinal juice more easily and rapidly than in model gastric juice. In addition, the capsules containing lactoferrin, an anti-carcinogenic protein, were found to keep 12.5% of the protein used in encapsulation without losing its activity.

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Section: Resultsmentioning

confidence: 99%

Preparation of tiny biodegradable capsules using electrocapillary emulsification

Abe

Nakayama²,

Kondo³

et al. 2007

Journal of Microencapsulation

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“…These occurrences may indicate elimination from more than one compartment. The MTHPA covalently bound to proteins may constitute a second slow compartment, since acid anhydrides are known to react with proteins (Palacian et al 1990;Johannesson et al 2001Johannesson et al , 2004. It is thought that such a second compartment would have had a greater influence in the urine from the chronically exposed workers than in the urine from the briefly exposed volunteers.…”

Section: Discussionmentioning

confidence: 99%

Methyltetrahydrophthalic acid in urine as an indicator of occupational exposure to methyltetrahydrophthalic anhydride

Yokota¹,

Johyama²,

Kunitani³

et al. 2005

Int Arch Occup Environ Health

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“…Following the protocol by Johannesson et al (2004) conjugates between KLH and HHPA were prepared at pH 8.1 and then dialyzed. KLH-HHPA antiserum was produced by immunizing a rabbit with repeated injections of these KLH-HHPA conjugates at Antibody AB (Lund, Sweden).…”

Section: Preparation and Purification Of Klh-hhpa Antiserummentioning

confidence: 99%

“…In previous studies, it has been shown that HSA is the major HHPA-binding protein in plasma (Johannesson et al, 2004). Thus, HSA was chosen as a relevant model carrier protein in the evaluation of the IAE column.…”

Section: Evaluation Of the Iae Columnmentioning

confidence: 99%

“…It has also been shown that HSA is the major site for in vivo formation of hapten-carrier protein adducts in plasma in humans . Also, some modified proteins using proteomics methodology have been identified in nasal lavage from exposed workers (Johannesson et al, 2004). However, only proteins in the high abundance range in plasma or nasal lavage have been identified.…”

Section: Future Usementioning

confidence: 99%

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Evaluation of an immunoaffinity extraction column for enrichment of adducts between human serum albumin and hexahydrophthalic anhydride in plasma

Johannesson

Kristiansson

Jönsson

et al. 2007

Biomedical Chromatography

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An immunoaffinity extraction (IAE) column was prepared for extraction of adducts between human serum albumin (HSA) and hexahydrophthalic anhydride (HHPA). HHPA is a strong sensitizer inducing immunoglobulin E antibodies in vivo. Polyclonal antibodies from a rabbit immunized with keyhole limpet hemocyananin-HHPA conjugate were purified using a Protein A Sepharose gel. To obtain antibodies with optimal affinity towards HHPA-protein adducts, HHPA-specific antibodies were selected using an N-hydroxysuccinimide-Sepharose column coupled with albumin-HHPA conjugate. Antibodies eluted from this column at pH 2.2 were selected to prepare the IAE column. The column was evaluated using 2 mL plasma spiked with HSA-HHPA conjugate. The column was eluted with glycine buffer at pH 2.0. The conjugates in the eluate were hydrolyzed to the corresponding HHP acid and quantified by mass spectrometry. The average recovery of HHPA adducts in 11 experiments was 68% with a coefficient of variation (CV) of 7%. The column's capacity to bind protein-HHPA adducts was found to be linear in the range of 0.15-1.2 nmol conjugate. The evaluation showed that the IAE column had adequate affinity towards the HHPA adducts and that the adducts could be extracted with good recovery and precision from a large volume of plasma.

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In vivo conjugation of nasal lavage proteins by hexahydrophthalic anhydride

Cited by 10 publications

References 43 publications

Preparation of tiny biodegradable capsules using electrocapillary emulsification

Preparation of tiny biodegradable capsules using electrocapillary emulsification

Methyltetrahydrophthalic acid in urine as an indicator of occupational exposure to methyltetrahydrophthalic anhydride

Evaluation of an immunoaffinity extraction column for enrichment of adducts between human serum albumin and hexahydrophthalic anhydride in plasma

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