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

Division of Biomedical Sciences

نتاج البحث: Article › مراجعة النظراء

5 اقتباسات (Scopus)

ملخص

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 2-3 M 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.

اللغة الأصلية	English
الصفحات (من إلى)	367-371
عدد الصفحات	5
دورية	Journal of Chromatography B: Biomedical Sciences and Applications
مستوى الصوت	755
رقم الإصدار	1-2
المعرِّفات الرقمية للأشياء	https://doi.org/10.1016/S0378-4347(01)00112-8
حالة النشر	Published - 1 مايو 2001

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10.1016/S0378-4347(01)00112-8

http://eprints.gla.ac.uk/128454/

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@article{bd46e2d4ae074c1a80cc966e2ae68079,

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 2-3 M 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.",

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

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

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T1 - Purification of factor X by hydrophobic interaction chromatography

AU - Husi, Holger

AU - Walkinshaw, Malcolm D.

PY - 2001/5/1

Y1 - 2001/5/1

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 2-3 M 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 2-3 M 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.

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

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

M3 - Article

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

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