A rainbow trout lectin with multimeric structure

Liselotte Jensen; Steffen Thiel; Torben E. Petersen; Jens C. Jensenius

doi:10.1016/S0305-0491(96)00273-8

A rainbow trout lectin with multimeric structure

Liselotte Jensen, Steffen Thiel, Torben E. Petersen, Jens C. Jensenius

Research output: Contribution to journal › Article › peer-review

51 Scopus citations

Abstract

A novel lectin has been identified in rainbow trout serum and plasma. The lectin binds to Sepharose (an agarose polymer) in a calcium-dependent manner. Glucose, N-acetyl-glucosamine, mannose, N-acetylmannosamine, L-fucose, maltose and α-methyl-mannoside are good inhibitors of this binding, whereas glucosamine and D-fucose inhibits to a lesser degree and mannosamine and galactose do not inhibit the binding to Sepharose. When analysed by SDS-PAGE under non-reducing conditions, the lectin appears as a characteristic ladder of bands with approximately 16 kDa between consecutive bands. Upon reduction, the lectin appears as a 16-kDa band. On size-exclusion chromatography of trout serum and plasma, the protein emerges over a broad range corresponding to sizes from about 2000 kDa to less than 200 kDa. The NH₂-terminal sequence (AAENRNQXPPG) shows no significant homology with known proteins. Because of the characteristic appearance in non-reducing SDS-PAGE and the lectin activity, we propose to name the protein 'ladderlectin'.

Original language	English
Pages (from-to)	385-390
Number of pages	6
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	116
Issue number	4
DOIs	https://doi.org/10.1016/S0305-0491(96)00273-8
State	Published - Apr 1997

Keywords

Animals
Blotting, Western
Calcium/metabolism
Carbohydrate Metabolism
Chromatography, Affinity/methods
Chromatography, Liquid/methods
Electrophoresis, Polyacrylamide Gel/methods
Fish Proteins
Lectins/immunology
Oncorhynchus mykiss/blood
Sequence Homology, Amino Acid
Substrate Specificity

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10.1016/S0305-0491(96)00273-8

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@article{daadccdf5f554378adfd3b97ed9b93ea,

title = "A rainbow trout lectin with multimeric structure",

abstract = "A novel lectin has been identified in rainbow trout serum and plasma. The lectin binds to Sepharose (an agarose polymer) in a calcium-dependent manner. Glucose, N-acetyl-glucosamine, mannose, N-acetylmannosamine, L-fucose, maltose and α-methyl-mannoside are good inhibitors of this binding, whereas glucosamine and D-fucose inhibits to a lesser degree and mannosamine and galactose do not inhibit the binding to Sepharose. When analysed by SDS-PAGE under non-reducing conditions, the lectin appears as a characteristic ladder of bands with approximately 16 kDa between consecutive bands. Upon reduction, the lectin appears as a 16-kDa band. On size-exclusion chromatography of trout serum and plasma, the protein emerges over a broad range corresponding to sizes from about 2000 kDa to less than 200 kDa. The NH2-terminal sequence (AAENRNQXPPG) shows no significant homology with known proteins. Because of the characteristic appearance in non-reducing SDS-PAGE and the lectin activity, we propose to name the protein 'ladderlectin'.",

keywords = "Animals, Blotting, Western, Calcium/metabolism, Carbohydrate Metabolism, Chromatography, Affinity/methods, Chromatography, Liquid/methods, Electrophoresis, Polyacrylamide Gel/methods, Fish Proteins, Lectins/immunology, Oncorhynchus mykiss/blood, Sequence Homology, Amino Acid, Substrate Specificity",

author = "Liselotte Jensen and Steffen Thiel and Petersen, {Torben E.} and Jensenius, {Jens C.}",

year = "1997",

month = apr,

doi = "10.1016/S0305-0491(96)00273-8",

language = "English",

volume = "116",

pages = "385--390",

journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",

issn = "0305-0491",

publisher = "Elsevier Inc.",

number = "4",

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TY - JOUR

T1 - A rainbow trout lectin with multimeric structure

AU - Jensen, Liselotte

AU - Thiel, Steffen

AU - Petersen, Torben E.

AU - Jensenius, Jens C.

PY - 1997/4

Y1 - 1997/4

N2 - A novel lectin has been identified in rainbow trout serum and plasma. The lectin binds to Sepharose (an agarose polymer) in a calcium-dependent manner. Glucose, N-acetyl-glucosamine, mannose, N-acetylmannosamine, L-fucose, maltose and α-methyl-mannoside are good inhibitors of this binding, whereas glucosamine and D-fucose inhibits to a lesser degree and mannosamine and galactose do not inhibit the binding to Sepharose. When analysed by SDS-PAGE under non-reducing conditions, the lectin appears as a characteristic ladder of bands with approximately 16 kDa between consecutive bands. Upon reduction, the lectin appears as a 16-kDa band. On size-exclusion chromatography of trout serum and plasma, the protein emerges over a broad range corresponding to sizes from about 2000 kDa to less than 200 kDa. The NH2-terminal sequence (AAENRNQXPPG) shows no significant homology with known proteins. Because of the characteristic appearance in non-reducing SDS-PAGE and the lectin activity, we propose to name the protein 'ladderlectin'.

AB - A novel lectin has been identified in rainbow trout serum and plasma. The lectin binds to Sepharose (an agarose polymer) in a calcium-dependent manner. Glucose, N-acetyl-glucosamine, mannose, N-acetylmannosamine, L-fucose, maltose and α-methyl-mannoside are good inhibitors of this binding, whereas glucosamine and D-fucose inhibits to a lesser degree and mannosamine and galactose do not inhibit the binding to Sepharose. When analysed by SDS-PAGE under non-reducing conditions, the lectin appears as a characteristic ladder of bands with approximately 16 kDa between consecutive bands. Upon reduction, the lectin appears as a 16-kDa band. On size-exclusion chromatography of trout serum and plasma, the protein emerges over a broad range corresponding to sizes from about 2000 kDa to less than 200 kDa. The NH2-terminal sequence (AAENRNQXPPG) shows no significant homology with known proteins. Because of the characteristic appearance in non-reducing SDS-PAGE and the lectin activity, we propose to name the protein 'ladderlectin'.

KW - Animals

KW - Blotting, Western

KW - Calcium/metabolism

KW - Carbohydrate Metabolism

KW - Chromatography, Affinity/methods

KW - Chromatography, Liquid/methods

KW - Electrophoresis, Polyacrylamide Gel/methods

KW - Fish Proteins

KW - Lectins/immunology

KW - Oncorhynchus mykiss/blood

KW - Sequence Homology, Amino Acid

KW - Substrate Specificity

UR - http://www.scopus.com/inward/record.url?scp=0031011541&partnerID=8YFLogxK

UR - http://europepmc.org/abstract/med/9149391

U2 - 10.1016/S0305-0491(96)00273-8

DO - 10.1016/S0305-0491(96)00273-8

M3 - Article

C2 - 9149391

SN - 0305-0491

VL - 116

SP - 385

EP - 390

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

IS - 4

ER -

A rainbow trout lectin with multimeric structure

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