Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors

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Standard

Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors. / Frøkiaer, Hanne; Hørlyck, Lene; Sørensen, Susanne; Sørensen, Hilmer.

I: Journal of the Science of Food and Agriculture, Bind 66, Nr. 1, 09.1994, s. 61-69.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Frøkiaer, H, Hørlyck, L, Sørensen, S & Sørensen, H 1994, 'Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors', Journal of the Science of Food and Agriculture, bind 66, nr. 1, s. 61-69. https://doi.org/10.1002/jsfa.2740660110

APA

Frøkiaer, H., Hørlyck, L., Sørensen, S., & Sørensen, H. (1994). Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors. Journal of the Science of Food and Agriculture, 66(1), 61-69. https://doi.org/10.1002/jsfa.2740660110

Vancouver

Frøkiaer H, Hørlyck L, Sørensen S, Sørensen H. Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors. Journal of the Science of Food and Agriculture. 1994 sep.;66(1):61-69. https://doi.org/10.1002/jsfa.2740660110

Author

Frøkiaer, Hanne ; Hørlyck, Lene ; Sørensen, Susanne ; Sørensen, Hilmer. / Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors. I: Journal of the Science of Food and Agriculture. 1994 ; Bind 66, Nr. 1. s. 61-69.

Bibtex

@article{f89dfab27f5444dca96c29aeedc75f3b,
title = "Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors",
abstract = "Trypsin inhibitors from pea (Pisum sativum (L) cultivar Progreta grown in Denmark) have been isolated and shown to consist of at least nine pea proteinase inhibitors (PPI) with inhibitor activity toward both trypsin and chymotrypsin. The isoelectric points of the inhibitors were in the range 4.9–7.8. From this PPI mixture at least four inhibitors were isolated by immunoaflinity chromatography on a column containing immobilised monoclonal antibody (mAb) with inhibitor specificity. The PPI isolated by immunoaffinity chromatography were further separated by HPLC, and subsequent SDS‐PAGE analysis showed molecular weights for four of the PPI in the range 11.3–14.2 kD. Their pI were determined by isoelectric focusing, mAbs were used for immunochemical characterisation and their amino acid composition showed a high (14.7–21%) content of cysteine. Tryptophan was not present in any of the isolated PPI. The data now obtained support the resemblance of PPI with inhibitors of the Bowman‐Birk class and the differences in immunochemical properties of the various PPI indicate that pea has at least two gene loci coding for the inhibitors.",
keywords = "immunoaflinity, amino acid composition, monoclonal antibodies, Pisum sativum L, trypsin inhibitors",
author = "Hanne Fr{\o}kiaer and Lene H{\o}rlyck and Susanne S{\o}rensen and Hilmer S{\o}rensen",
year = "1994",
month = sep,
doi = "10.1002/jsfa.2740660110",
language = "English",
volume = "66",
pages = "61--69",
journal = "Journal of the Science of Food and Agriculture",
issn = "0022-5142",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Immunoaffinity chromatography purification and characterisation of pea trypsin inhibitors

AU - Frøkiaer, Hanne

AU - Hørlyck, Lene

AU - Sørensen, Susanne

AU - Sørensen, Hilmer

PY - 1994/9

Y1 - 1994/9

N2 - Trypsin inhibitors from pea (Pisum sativum (L) cultivar Progreta grown in Denmark) have been isolated and shown to consist of at least nine pea proteinase inhibitors (PPI) with inhibitor activity toward both trypsin and chymotrypsin. The isoelectric points of the inhibitors were in the range 4.9–7.8. From this PPI mixture at least four inhibitors were isolated by immunoaflinity chromatography on a column containing immobilised monoclonal antibody (mAb) with inhibitor specificity. The PPI isolated by immunoaffinity chromatography were further separated by HPLC, and subsequent SDS‐PAGE analysis showed molecular weights for four of the PPI in the range 11.3–14.2 kD. Their pI were determined by isoelectric focusing, mAbs were used for immunochemical characterisation and their amino acid composition showed a high (14.7–21%) content of cysteine. Tryptophan was not present in any of the isolated PPI. The data now obtained support the resemblance of PPI with inhibitors of the Bowman‐Birk class and the differences in immunochemical properties of the various PPI indicate that pea has at least two gene loci coding for the inhibitors.

AB - Trypsin inhibitors from pea (Pisum sativum (L) cultivar Progreta grown in Denmark) have been isolated and shown to consist of at least nine pea proteinase inhibitors (PPI) with inhibitor activity toward both trypsin and chymotrypsin. The isoelectric points of the inhibitors were in the range 4.9–7.8. From this PPI mixture at least four inhibitors were isolated by immunoaflinity chromatography on a column containing immobilised monoclonal antibody (mAb) with inhibitor specificity. The PPI isolated by immunoaffinity chromatography were further separated by HPLC, and subsequent SDS‐PAGE analysis showed molecular weights for four of the PPI in the range 11.3–14.2 kD. Their pI were determined by isoelectric focusing, mAbs were used for immunochemical characterisation and their amino acid composition showed a high (14.7–21%) content of cysteine. Tryptophan was not present in any of the isolated PPI. The data now obtained support the resemblance of PPI with inhibitors of the Bowman‐Birk class and the differences in immunochemical properties of the various PPI indicate that pea has at least two gene loci coding for the inhibitors.

KW - immunoaflinity, amino acid composition

KW - monoclonal antibodies

KW - Pisum sativum L

KW - trypsin inhibitors

UR - http://www.scopus.com/inward/record.url?scp=0028005574&partnerID=8YFLogxK

U2 - 10.1002/jsfa.2740660110

DO - 10.1002/jsfa.2740660110

M3 - Journal article

AN - SCOPUS:0028005574

VL - 66

SP - 61

EP - 69

JO - Journal of the Science of Food and Agriculture

JF - Journal of the Science of Food and Agriculture

SN - 0022-5142

IS - 1

ER -

ID: 331795117