Purification of factor X by hydrophobic interaction chromatography

Holger Husi; Malcolm D. Walkinshaw

doi:10.1016/S0378-4347(01)00112-8

Purification of factor X by hydrophobic interaction chromatography

Holger Husi, Malcolm D. Walkinshaw

Research output: Journal Publication › Article › peer-review

5 Citations (Scopus)

Abstract

Human factor X has been purified to homogeneity by hydrophobic interaction chromatography on phenyl-sepharose. The coagulation protein did not interact with the resin in the presence of 2-3M NaCl whereas contaminants were retained. This single purification step, in conjunction with classical purification strategies, is a powerful tool in generating high purity factor X and is based on resins which are readily available.

Original language	English
Pages (from-to)	367-371
Number of pages	5
Journal	Journal of Chromatography B: Biomedical Sciences and Applications
Volume	755
Issue number	1-2
DOIs	https://doi.org/10.1016/S0378-4347(01)00112-8
Publication status	Published - 5 May 2001
Externally published	Yes

Keywords

Factor X
Purification

ASJC Scopus subject areas

General Chemistry

Access to Document

10.1016/S0378-4347(01)00112-8

Cite this

@article{bbb04ecbbfa749b59eeba35244380f97,

title = "Purification of factor X by hydrophobic interaction chromatography",

abstract = "Human factor X has been purified to homogeneity by hydrophobic interaction chromatography on phenyl-sepharose. The coagulation protein did not interact with the resin in the presence of 2-3M NaCl whereas contaminants were retained. This single purification step, in conjunction with classical purification strategies, is a powerful tool in generating high purity factor X and is based on resins which are readily available.",

keywords = "Factor X, Purification",

author = "Holger Husi and Walkinshaw, \{Malcolm D.\}",

year = "2001",

month = may,

day = "5",

doi = "10.1016/S0378-4347(01)00112-8",

language = "English",

volume = "755",

pages = "367--371",

journal = "Journal of Chromatography B: Biomedical Sciences and Applications",

issn = "1387-2273",

publisher = "Elsevier B.V.",

number = "1-2",

}

TY - JOUR

T1 - Purification of factor X by hydrophobic interaction chromatography

AU - Husi, Holger

AU - Walkinshaw, Malcolm D.

PY - 2001/5/5

Y1 - 2001/5/5

N2 - Human factor X has been purified to homogeneity by hydrophobic interaction chromatography on phenyl-sepharose. The coagulation protein did not interact with the resin in the presence of 2-3M NaCl whereas contaminants were retained. This single purification step, in conjunction with classical purification strategies, is a powerful tool in generating high purity factor X and is based on resins which are readily available.

AB - Human factor X has been purified to homogeneity by hydrophobic interaction chromatography on phenyl-sepharose. The coagulation protein did not interact with the resin in the presence of 2-3M NaCl whereas contaminants were retained. This single purification step, in conjunction with classical purification strategies, is a powerful tool in generating high purity factor X and is based on resins which are readily available.

KW - Factor X

KW - Purification

UR - https://www.scopus.com/pages/publications/0035810731

U2 - 10.1016/S0378-4347(01)00112-8

DO - 10.1016/S0378-4347(01)00112-8

M3 - Article

C2 - 11393727

AN - SCOPUS:0035810731

SN - 1387-2273

VL - 755

SP - 367

EP - 371

JO - Journal of Chromatography B: Biomedical Sciences and Applications

JF - Journal of Chromatography B: Biomedical Sciences and Applications

IS - 1-2

ER -

Purification of factor X by hydrophobic interaction chromatography

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this