A high yield purification of the human transferrin receptor and properties of its major extracellular fragment

A. P. Turkewitz, J. F. Amatruda, D. Borhani, S. C. Harrison, A. L. Schwartz

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

Human transferrin receptor is a disulfide-linked homodimer of 90-kDa glycoprotein subunits, capable of binding two transferrins. We report a new high yield affinity purification protocol for transferrin receptor from placenta which produces 3-4 mg of highly purified protein. Trypsin cleaves the protein at arginine-121, producing a stable fragment that contains 95% of the extracytoplasmic sequence; similar fragments are produced by several other proteases. The tryptic fragment is a nondisulfide-linked dimer in solution and binds two transferrin molecules. The dimensions of both the dimer fragment and its complex with transferrin are estimated by gel filtration.

Original languageEnglish (US)
Pages (from-to)8318-8325
Number of pages8
JournalJournal of Biological Chemistry
Volume263
Issue number17
StatePublished - 1988

Fingerprint

Transferrin Receptors
Transferrin
Dimers
Purification
Transferrins
Disulfides
Trypsin
Placenta
Gel Chromatography
Arginine
Glycoproteins
Proteins
Peptide Hydrolases
Gels
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Turkewitz, A. P., Amatruda, J. F., Borhani, D., Harrison, S. C., & Schwartz, A. L. (1988). A high yield purification of the human transferrin receptor and properties of its major extracellular fragment. Journal of Biological Chemistry, 263(17), 8318-8325.

A high yield purification of the human transferrin receptor and properties of its major extracellular fragment. / Turkewitz, A. P.; Amatruda, J. F.; Borhani, D.; Harrison, S. C.; Schwartz, A. L.

In: Journal of Biological Chemistry, Vol. 263, No. 17, 1988, p. 8318-8325.

Research output: Contribution to journalArticle

Turkewitz, AP, Amatruda, JF, Borhani, D, Harrison, SC & Schwartz, AL 1988, 'A high yield purification of the human transferrin receptor and properties of its major extracellular fragment', Journal of Biological Chemistry, vol. 263, no. 17, pp. 8318-8325.
Turkewitz, A. P. ; Amatruda, J. F. ; Borhani, D. ; Harrison, S. C. ; Schwartz, A. L. / A high yield purification of the human transferrin receptor and properties of its major extracellular fragment. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 17. pp. 8318-8325.
@article{37beb42ef2ca4a61a6512b673eb80b84,
title = "A high yield purification of the human transferrin receptor and properties of its major extracellular fragment",
abstract = "Human transferrin receptor is a disulfide-linked homodimer of 90-kDa glycoprotein subunits, capable of binding two transferrins. We report a new high yield affinity purification protocol for transferrin receptor from placenta which produces 3-4 mg of highly purified protein. Trypsin cleaves the protein at arginine-121, producing a stable fragment that contains 95{\%} of the extracytoplasmic sequence; similar fragments are produced by several other proteases. The tryptic fragment is a nondisulfide-linked dimer in solution and binds two transferrin molecules. The dimensions of both the dimer fragment and its complex with transferrin are estimated by gel filtration.",
author = "Turkewitz, {A. P.} and Amatruda, {J. F.} and D. Borhani and Harrison, {S. C.} and Schwartz, {A. L.}",
year = "1988",
language = "English (US)",
volume = "263",
pages = "8318--8325",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "17",

}

TY - JOUR

T1 - A high yield purification of the human transferrin receptor and properties of its major extracellular fragment

AU - Turkewitz, A. P.

AU - Amatruda, J. F.

AU - Borhani, D.

AU - Harrison, S. C.

AU - Schwartz, A. L.

PY - 1988

Y1 - 1988

N2 - Human transferrin receptor is a disulfide-linked homodimer of 90-kDa glycoprotein subunits, capable of binding two transferrins. We report a new high yield affinity purification protocol for transferrin receptor from placenta which produces 3-4 mg of highly purified protein. Trypsin cleaves the protein at arginine-121, producing a stable fragment that contains 95% of the extracytoplasmic sequence; similar fragments are produced by several other proteases. The tryptic fragment is a nondisulfide-linked dimer in solution and binds two transferrin molecules. The dimensions of both the dimer fragment and its complex with transferrin are estimated by gel filtration.

AB - Human transferrin receptor is a disulfide-linked homodimer of 90-kDa glycoprotein subunits, capable of binding two transferrins. We report a new high yield affinity purification protocol for transferrin receptor from placenta which produces 3-4 mg of highly purified protein. Trypsin cleaves the protein at arginine-121, producing a stable fragment that contains 95% of the extracytoplasmic sequence; similar fragments are produced by several other proteases. The tryptic fragment is a nondisulfide-linked dimer in solution and binds two transferrin molecules. The dimensions of both the dimer fragment and its complex with transferrin are estimated by gel filtration.

UR - http://www.scopus.com/inward/record.url?scp=0023899377&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023899377&partnerID=8YFLogxK

M3 - Article

C2 - 3372526

AN - SCOPUS:0023899377

VL - 263

SP - 8318

EP - 8325

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 17

ER -