Aarhus University Seal / Aarhus Universitets segl

Jens Christian Jensenius

Isolation of a pentraxin-like protein from rainbow trout serum

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

Standard

Isolation of a pentraxin-like protein from rainbow trout serum. / Jensen, L E; Petersen, T E; Thiel, S; Jensenius, J C.

In: Developmental & Comparative Immunology, Vol. 19, No. 4, 1995, p. 305-14.

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

Harvard

Jensen, LE, Petersen, TE, Thiel, S & Jensenius, JC 1995, 'Isolation of a pentraxin-like protein from rainbow trout serum', Developmental & Comparative Immunology, vol. 19, no. 4, pp. 305-14.

APA

Jensen, L. E., Petersen, T. E., Thiel, S., & Jensenius, J. C. (1995). Isolation of a pentraxin-like protein from rainbow trout serum. Developmental & Comparative Immunology, 19(4), 305-14.

CBE

Jensen LE, Petersen TE, Thiel S, Jensenius JC. 1995. Isolation of a pentraxin-like protein from rainbow trout serum. Developmental & Comparative Immunology. 19(4):305-14.

MLA

Jensen, L E et al. "Isolation of a pentraxin-like protein from rainbow trout serum". Developmental & Comparative Immunology. 1995, 19(4). 305-14.

Vancouver

Jensen LE, Petersen TE, Thiel S, Jensenius JC. Isolation of a pentraxin-like protein from rainbow trout serum. Developmental & Comparative Immunology. 1995;19(4):305-14.

Author

Jensen, L E ; Petersen, T E ; Thiel, S ; Jensenius, J C. / Isolation of a pentraxin-like protein from rainbow trout serum. In: Developmental & Comparative Immunology. 1995 ; Vol. 19, No. 4. pp. 305-14.

Bibtex

@article{84275612de0a482caa0495051a2e278d,
title = "Isolation of a pentraxin-like protein from rainbow trout serum",
abstract = "Serum amyloid P-component (SAP) is a glycoprotein consisting of five or ten noncovalently associated identical subunits of molecular weight 19,000-30,000. Herein we report the isolation and partial characterization of a SAP-like protein from rainbow trout serum. The protein was isolated by calcium-dependent binding to Sepharose followed by ion-exchange and size-exclusion chromatography. Rabbit antibody against human SAP reacted with the trout protein and the NH2-terminal sequence of 16 amino acids showed 60{\%} identity with the first 15 residues of human SAP. SDS-PAGE and endoglycosidase treatment indicated that the trout protein is a glycoprotein in which five or six subunits are linked by disulphide bonds. The subunits have a molecular weight of 37,000 of which approximately 13{\%} is due to carbohydrate. We propose to name the trout protein sulphide linked SAP (SL-SAP).",
keywords = "Alpha-Globulins, Amino Acid Sequence, Animals, C-Reactive Protein, Glycosylation, Humans, Molecular Sequence Data, Molecular Weight, Oncorhynchus mykiss, Protein Binding, Rabbits, Sepharose, Sequence Homology, Amino Acid, Serum Amyloid P-Component",
author = "Jensen, {L E} and Petersen, {T E} and S Thiel and Jensenius, {J C}",
year = "1995",
language = "English",
volume = "19",
pages = "305--14",
journal = "Developmental & Comparative Immunology",
issn = "0145-305X",
publisher = "Pergamon Press",
number = "4",

}

RIS

TY - JOUR

T1 - Isolation of a pentraxin-like protein from rainbow trout serum

AU - Jensen, L E

AU - Petersen, T E

AU - Thiel, S

AU - Jensenius, J C

PY - 1995

Y1 - 1995

N2 - Serum amyloid P-component (SAP) is a glycoprotein consisting of five or ten noncovalently associated identical subunits of molecular weight 19,000-30,000. Herein we report the isolation and partial characterization of a SAP-like protein from rainbow trout serum. The protein was isolated by calcium-dependent binding to Sepharose followed by ion-exchange and size-exclusion chromatography. Rabbit antibody against human SAP reacted with the trout protein and the NH2-terminal sequence of 16 amino acids showed 60% identity with the first 15 residues of human SAP. SDS-PAGE and endoglycosidase treatment indicated that the trout protein is a glycoprotein in which five or six subunits are linked by disulphide bonds. The subunits have a molecular weight of 37,000 of which approximately 13% is due to carbohydrate. We propose to name the trout protein sulphide linked SAP (SL-SAP).

AB - Serum amyloid P-component (SAP) is a glycoprotein consisting of five or ten noncovalently associated identical subunits of molecular weight 19,000-30,000. Herein we report the isolation and partial characterization of a SAP-like protein from rainbow trout serum. The protein was isolated by calcium-dependent binding to Sepharose followed by ion-exchange and size-exclusion chromatography. Rabbit antibody against human SAP reacted with the trout protein and the NH2-terminal sequence of 16 amino acids showed 60% identity with the first 15 residues of human SAP. SDS-PAGE and endoglycosidase treatment indicated that the trout protein is a glycoprotein in which five or six subunits are linked by disulphide bonds. The subunits have a molecular weight of 37,000 of which approximately 13% is due to carbohydrate. We propose to name the trout protein sulphide linked SAP (SL-SAP).

KW - Alpha-Globulins

KW - Amino Acid Sequence

KW - Animals

KW - C-Reactive Protein

KW - Glycosylation

KW - Humans

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Oncorhynchus mykiss

KW - Protein Binding

KW - Rabbits

KW - Sepharose

KW - Sequence Homology, Amino Acid

KW - Serum Amyloid P-Component

M3 - Journal article

C2 - 8617401

VL - 19

SP - 305

EP - 314

JO - Developmental & Comparative Immunology

JF - Developmental & Comparative Immunology

SN - 0145-305X

IS - 4

ER -