Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor : a novel plasma protein structure. / Jessen, T E; Faarvang, K L; Ploug, M.

In: FEBS Letters, Vol. 230, No. 1-2, 28.03.1988, p. 195-200.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Jessen, TE, Faarvang, KL & Ploug, M 1988, 'Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure', FEBS Letters, vol. 230, no. 1-2, pp. 195-200.

APA

Jessen, T. E., Faarvang, K. L., & Ploug, M. (1988). Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure. FEBS Letters, 230(1-2), 195-200.

Vancouver

Jessen TE, Faarvang KL, Ploug M. Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure. FEBS Letters. 1988 Mar 28;230(1-2):195-200.

Author

Jessen, T E ; Faarvang, K L ; Ploug, M. / Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor : a novel plasma protein structure. In: FEBS Letters. 1988 ; Vol. 230, No. 1-2. pp. 195-200.

Bibtex

@article{ab099d1e11a443468bdf50909e5a17d3,
title = "Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure",
abstract = "The primary structure of inter-alpha-trypsin inhibitor is partially elucidated, but controversy about the construction of the polypeptide backbone still exists. We present evidence suggesting that inter-alpha-trypsin inhibitor represents a novel plasma protein structure with two separate polypeptide chains covalently crosslinked only by carbohydrate (chondroitin sulphate).",
keywords = "Alpha-Globulins, Amino Acid Sequence, Carbohydrates, Chondroitin Lyases, Chondroitin Sulfates, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Humans, Hyaluronoglucosaminidase, Immunoelectrophoresis, Immunosorbent Techniques, Molecular Sequence Data, Molecular Weight, Trypsin Inhibitors, Journal Article",
author = "Jessen, {T E} and Faarvang, {K L} and M Ploug",
year = "1988",
month = mar,
day = "28",
language = "English",
volume = "230",
pages = "195--200",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-2",

}

RIS

TY - JOUR

T1 - Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor

T2 - a novel plasma protein structure

AU - Jessen, T E

AU - Faarvang, K L

AU - Ploug, M

PY - 1988/3/28

Y1 - 1988/3/28

N2 - The primary structure of inter-alpha-trypsin inhibitor is partially elucidated, but controversy about the construction of the polypeptide backbone still exists. We present evidence suggesting that inter-alpha-trypsin inhibitor represents a novel plasma protein structure with two separate polypeptide chains covalently crosslinked only by carbohydrate (chondroitin sulphate).

AB - The primary structure of inter-alpha-trypsin inhibitor is partially elucidated, but controversy about the construction of the polypeptide backbone still exists. We present evidence suggesting that inter-alpha-trypsin inhibitor represents a novel plasma protein structure with two separate polypeptide chains covalently crosslinked only by carbohydrate (chondroitin sulphate).

KW - Alpha-Globulins

KW - Amino Acid Sequence

KW - Carbohydrates

KW - Chondroitin Lyases

KW - Chondroitin Sulfates

KW - Chromatography, Gel

KW - Electrophoresis, Polyacrylamide Gel

KW - Humans

KW - Hyaluronoglucosaminidase

KW - Immunoelectrophoresis

KW - Immunosorbent Techniques

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Trypsin Inhibitors

KW - Journal Article

M3 - Journal article

C2 - 2450785

VL - 230

SP - 195

EP - 200

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-2

ER -

ID: 178214818