Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.).

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Standard

Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.). / Kofod, H.; Pedersen, K.; Larsen, J. L.; Buchmann, K.

I: Acta Veterinaria Scandinavica, Bind 35, Nr. 1, 1994, s. 1-10.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Kofod, H, Pedersen, K, Larsen, JL & Buchmann, K 1994, 'Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.).', Acta Veterinaria Scandinavica, bind 35, nr. 1, s. 1-10.

APA

Kofod, H., Pedersen, K., Larsen, J. L., & Buchmann, K. (1994). Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.). Acta Veterinaria Scandinavica, 35(1), 1-10.

Vancouver

Kofod H, Pedersen K, Larsen JL, Buchmann K. Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.). Acta Veterinaria Scandinavica. 1994;35(1):1-10.

Author

Kofod, H. ; Pedersen, K. ; Larsen, J. L. ; Buchmann, K. / Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.). I: Acta Veterinaria Scandinavica. 1994 ; Bind 35, Nr. 1. s. 1-10.

Bibtex

@article{1ac9d600bc06401cb5c7aac70d9da8a0,
title = "Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.).",
abstract = "A total of 40 turbot (Scophthalmus maximus) were immunized 3 times during a 3 months period using DNP-HSA whereafter serum samples were collected and pooled. Specific immunoglobulins (Ig) were affinity purified on an agarose column with immobilized DNP-BSA and further purified by gel filtration whereafter monospecific rabbit anti Ig serum was generated. Size exclusion chromatography and non-reduced SDS-PAGE indicated a MW of 8-900 kDa of the dominant antigen binding proteins from turbot serum. Reduced SDS-PAGE showed this fraction to be composed of disulphide linked heavy and light chains with MWs of 79 and 27-29 kDa, respectively, indicating a tetrameric structure. Isoelectric focusing of the 800-900 kDa Ig showed several bands between pH 5.5 and pH 5.8. Mean Ig concentration in serum of 10 turbot was measured to 6.48 mg/ml (SD 5.4) using rocket immunoelectrophoresis. Low molecular weight antigen binding molecules were copurified with the dominating immunoglobulins with an estimated MW of 500 kDa. Reducing SDS-PAGE of this fraction revealed molecules with MWs of 97, 79, 57, 29, and 27 kDa.",
author = "H. Kofod and K. Pedersen and Larsen, {J. L.} and K. Buchmann",
year = "1994",
language = "English",
volume = "35",
pages = "1--10",
journal = "Acta Veterinaria Scandinavica, Supplement",
issn = "0065-1699",
publisher = "DenDanske Dyrlaegeforening",
number = "1",

}

RIS

TY - JOUR

T1 - Purification and characterization of IgM-like immunoglobulin from turbot (Scophthalmus maximus L.).

AU - Kofod, H.

AU - Pedersen, K.

AU - Larsen, J. L.

AU - Buchmann, K.

PY - 1994

Y1 - 1994

N2 - A total of 40 turbot (Scophthalmus maximus) were immunized 3 times during a 3 months period using DNP-HSA whereafter serum samples were collected and pooled. Specific immunoglobulins (Ig) were affinity purified on an agarose column with immobilized DNP-BSA and further purified by gel filtration whereafter monospecific rabbit anti Ig serum was generated. Size exclusion chromatography and non-reduced SDS-PAGE indicated a MW of 8-900 kDa of the dominant antigen binding proteins from turbot serum. Reduced SDS-PAGE showed this fraction to be composed of disulphide linked heavy and light chains with MWs of 79 and 27-29 kDa, respectively, indicating a tetrameric structure. Isoelectric focusing of the 800-900 kDa Ig showed several bands between pH 5.5 and pH 5.8. Mean Ig concentration in serum of 10 turbot was measured to 6.48 mg/ml (SD 5.4) using rocket immunoelectrophoresis. Low molecular weight antigen binding molecules were copurified with the dominating immunoglobulins with an estimated MW of 500 kDa. Reducing SDS-PAGE of this fraction revealed molecules with MWs of 97, 79, 57, 29, and 27 kDa.

AB - A total of 40 turbot (Scophthalmus maximus) were immunized 3 times during a 3 months period using DNP-HSA whereafter serum samples were collected and pooled. Specific immunoglobulins (Ig) were affinity purified on an agarose column with immobilized DNP-BSA and further purified by gel filtration whereafter monospecific rabbit anti Ig serum was generated. Size exclusion chromatography and non-reduced SDS-PAGE indicated a MW of 8-900 kDa of the dominant antigen binding proteins from turbot serum. Reduced SDS-PAGE showed this fraction to be composed of disulphide linked heavy and light chains with MWs of 79 and 27-29 kDa, respectively, indicating a tetrameric structure. Isoelectric focusing of the 800-900 kDa Ig showed several bands between pH 5.5 and pH 5.8. Mean Ig concentration in serum of 10 turbot was measured to 6.48 mg/ml (SD 5.4) using rocket immunoelectrophoresis. Low molecular weight antigen binding molecules were copurified with the dominating immunoglobulins with an estimated MW of 500 kDa. Reducing SDS-PAGE of this fraction revealed molecules with MWs of 97, 79, 57, 29, and 27 kDa.

UR - http://www.scopus.com/inward/record.url?scp=0028252315&partnerID=8YFLogxK

M3 - Journal article

C2 - 8209813

AN - SCOPUS:0028252315

VL - 35

SP - 1

EP - 10

JO - Acta Veterinaria Scandinavica, Supplement

JF - Acta Veterinaria Scandinavica, Supplement

SN - 0065-1699

IS - 1

ER -

ID: 247152078