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Jens Christian Jensenius

Purification and characterization of mannan-binding protein from mouse serum

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Standard

Purification and characterization of mannan-binding protein from mouse serum. / Holt, P; Holmskov, U; Thiel, S; Teisner, B; Højrup, P; Jensenius, J C.

In: Scandinavian Journal of Immunology, Vol. 39, No. 2, 01.02.1994, p. 202-8.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Holt, P, Holmskov, U, Thiel, S, Teisner, B, Højrup, P & Jensenius, JC 1994, 'Purification and characterization of mannan-binding protein from mouse serum', Scandinavian Journal of Immunology, vol. 39, no. 2, pp. 202-8.

APA

Holt, P., Holmskov, U., Thiel, S., Teisner, B., Højrup, P., & Jensenius, J. C. (1994). Purification and characterization of mannan-binding protein from mouse serum. Scandinavian Journal of Immunology, 39(2), 202-8.

CBE

Holt P, Holmskov U, Thiel S, Teisner B, Højrup P, Jensenius JC. 1994. Purification and characterization of mannan-binding protein from mouse serum. Scandinavian Journal of Immunology. 39(2):202-8.

MLA

Holt, P et al. "Purification and characterization of mannan-binding protein from mouse serum". Scandinavian Journal of Immunology. 1994, 39(2). 202-8.

Vancouver

Holt P, Holmskov U, Thiel S, Teisner B, Højrup P, Jensenius JC. Purification and characterization of mannan-binding protein from mouse serum. Scandinavian Journal of Immunology. 1994 Feb 1;39(2):202-8.

Author

Holt, P ; Holmskov, U ; Thiel, S ; Teisner, B ; Højrup, P ; Jensenius, J C. / Purification and characterization of mannan-binding protein from mouse serum. In: Scandinavian Journal of Immunology. 1994 ; Vol. 39, No. 2. pp. 202-8.

Bibtex

@article{cab6415b724649bd9062f2424c0d0ade,
title = "Purification and characterization of mannan-binding protein from mouse serum",
abstract = "Mouse mannan-binding protein (MBP) was identified in serum by its Ca(2+)-dependent binding to mannan. On gel permeation chromatography, the protein eluted corresponding to a molecular weight of approximately 750 kDa. Analysed on SDS-PAGE under reducing conditions, the polypeptide showed an apparent molecular weight of 28 kDa, while several high molecular weight bands were seen under non-reducing conditions. The presence of collagen-like domains within the molecule was indicated by a high glycine content (14.9%) and substantiated by sensitivity to collagenase. Rabbit anti-mouse MBP antisera were raised. The concentration of MBP in serum from normal mice was measured by rocket immunoelectrophoresis and found to be from below 1 microgram/ml to 100 micrograms/ml (average 50 micrograms/ml, n = 60). The binding of mouse MBP to mannan could be inhibited by mono- and disaccharides in the following order of potency: L-fucose > D-mannose > N-acetyl-D-glucosamine > maltose > D-mannoheptulose > D-glucose > N-acetyl-D-mannosamine >> lactose > D-galactose >> N-acetyl-D-galactosamine. Mouse MBP was shown to activate the classical complement cascade after binding to mannan. The sequence of 14 NH2-terminal amino acid residues of the molecule showed 93% identity to rat MBP-A and complete identity to the translated cDNA sequences for mouse MBP-A and mouse Ra-reactive factor component P28b (RaRF P28b) published previously. The amino acid composition of mouse MBP showed a high degree of homology to MBPs from other species and mouse RaRF P28b.",
keywords = "Amino Acid Sequence, Amino Acids, Animals, Blood Protein Electrophoresis, Carrier Proteins, Chromatography, Gel, Collectins, Complement Pathway, Classical, Disaccharides, Mannans, Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Mice, Inbred Strains, Molecular Sequence Data, Molecular Weight, Monosaccharides",
author = "P Holt and U Holmskov and S Thiel and B Teisner and P H{\o}jrup and Jensenius, {J C}",
year = "1994",
month = feb,
day = "1",
language = "English",
volume = "39",
pages = "202--8",
journal = "Scandinavian Journal of Immunology",
issn = "0300-9475",
publisher = "Wiley-Blackwell Publishing Ltd.",
number = "2",

}

RIS

TY - JOUR

T1 - Purification and characterization of mannan-binding protein from mouse serum

AU - Holt, P

AU - Holmskov, U

AU - Thiel, S

AU - Teisner, B

AU - Højrup, P

AU - Jensenius, J C

PY - 1994/2/1

Y1 - 1994/2/1

N2 - Mouse mannan-binding protein (MBP) was identified in serum by its Ca(2+)-dependent binding to mannan. On gel permeation chromatography, the protein eluted corresponding to a molecular weight of approximately 750 kDa. Analysed on SDS-PAGE under reducing conditions, the polypeptide showed an apparent molecular weight of 28 kDa, while several high molecular weight bands were seen under non-reducing conditions. The presence of collagen-like domains within the molecule was indicated by a high glycine content (14.9%) and substantiated by sensitivity to collagenase. Rabbit anti-mouse MBP antisera were raised. The concentration of MBP in serum from normal mice was measured by rocket immunoelectrophoresis and found to be from below 1 microgram/ml to 100 micrograms/ml (average 50 micrograms/ml, n = 60). The binding of mouse MBP to mannan could be inhibited by mono- and disaccharides in the following order of potency: L-fucose > D-mannose > N-acetyl-D-glucosamine > maltose > D-mannoheptulose > D-glucose > N-acetyl-D-mannosamine >> lactose > D-galactose >> N-acetyl-D-galactosamine. Mouse MBP was shown to activate the classical complement cascade after binding to mannan. The sequence of 14 NH2-terminal amino acid residues of the molecule showed 93% identity to rat MBP-A and complete identity to the translated cDNA sequences for mouse MBP-A and mouse Ra-reactive factor component P28b (RaRF P28b) published previously. The amino acid composition of mouse MBP showed a high degree of homology to MBPs from other species and mouse RaRF P28b.

AB - Mouse mannan-binding protein (MBP) was identified in serum by its Ca(2+)-dependent binding to mannan. On gel permeation chromatography, the protein eluted corresponding to a molecular weight of approximately 750 kDa. Analysed on SDS-PAGE under reducing conditions, the polypeptide showed an apparent molecular weight of 28 kDa, while several high molecular weight bands were seen under non-reducing conditions. The presence of collagen-like domains within the molecule was indicated by a high glycine content (14.9%) and substantiated by sensitivity to collagenase. Rabbit anti-mouse MBP antisera were raised. The concentration of MBP in serum from normal mice was measured by rocket immunoelectrophoresis and found to be from below 1 microgram/ml to 100 micrograms/ml (average 50 micrograms/ml, n = 60). The binding of mouse MBP to mannan could be inhibited by mono- and disaccharides in the following order of potency: L-fucose > D-mannose > N-acetyl-D-glucosamine > maltose > D-mannoheptulose > D-glucose > N-acetyl-D-mannosamine >> lactose > D-galactose >> N-acetyl-D-galactosamine. Mouse MBP was shown to activate the classical complement cascade after binding to mannan. The sequence of 14 NH2-terminal amino acid residues of the molecule showed 93% identity to rat MBP-A and complete identity to the translated cDNA sequences for mouse MBP-A and mouse Ra-reactive factor component P28b (RaRF P28b) published previously. The amino acid composition of mouse MBP showed a high degree of homology to MBPs from other species and mouse RaRF P28b.

KW - Amino Acid Sequence

KW - Amino Acids

KW - Animals

KW - Blood Protein Electrophoresis

KW - Carrier Proteins

KW - Chromatography, Gel

KW - Collectins

KW - Complement Pathway, Classical

KW - Disaccharides

KW - Mannans

KW - Mice

KW - Mice, Inbred BALB C

KW - Mice, Inbred C57BL

KW - Mice, Inbred Strains

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Monosaccharides

M3 - Journal article

C2 - 8296164

VL - 39

SP - 202

EP - 208

JO - Scandinavian Journal of Immunology

JF - Scandinavian Journal of Immunology

SN - 0300-9475

IS - 2

ER -