scholarly journals Native Hydrophobic Interaction Chromatography Hyphenated to Mass Spectrometry for Characterization of Monoclonal Antibody Minor Variants

2019 ◽  
Vol 91 (24) ◽  
pp. 15360-15364 ◽  
Author(s):  
Bingchuan Wei ◽  
Guanghui Han ◽  
Jia Tang ◽  
Wendy Sandoval ◽  
Yonghua Taylor Zhang
Keyword(s):  
Mass Spectrometry ◽  
Monoclonal Antibody ◽  
Hydrophobic Interaction ◽  
Hydrophobic Interaction Chromatography

An improved capillary isoelectric focusing-mass spectrometry method for high-resolution characterization of monoclonal antibody charge variants

2022 ◽  
Author(s):  
Tian Xu ◽  
Linjie Han ◽  
Alayna M. George Thompson ◽  
Liangliang Sun
Keyword(s):  
Mass Spectrometry ◽  
Monoclonal Antibody ◽  
High Resolution ◽  
Isoelectric Focusing ◽  
Capillary Isoelectric Focusing ◽  
Spectrometry Method ◽  
Mass Spectrometry Method ◽  
Charge Variants

Routine and high-resolution characterization of monoclonal antibody (mAb) charge variants is vital for controlling mAb quality as therapeutics. Capillary isoelectric focusing-mass spectrometry (cIEF-MS) has emerged as a powerful tool for...

scholarly journals Detailed Characterization of Monoclonal Antibody Receptor Interaction Using Affinity Liquid Chromatography Hyphenated to Native Mass Spectrometry

2017 ◽  
Vol 89 (10) ◽  
pp. 5404-5412 ◽  
Author(s):  
Rabah Gahoual ◽  
Anna-Katharina Heidenreich ◽  
Govert W. Somsen ◽  
Patrick Bulau ◽  
Dietmar Reusch ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Monoclonal Antibody ◽  
Liquid Chromatography ◽  
Native Mass Spectrometry ◽  
Receptor Interaction ◽  
Detailed Characterization

Purification, immobilization and characterization of thermostable α-amylase from a thermophilic bacterium Geobacillus sp. TF14

2017 ◽  
Vol 42 (6) ◽  
Author(s):  
Şaban Keskin ◽  
Nagihan Saglam Ertunga
Keyword(s):  
Ion Exchange ◽  
Hydrophobic Interaction ◽  
Hydrophobic Interaction Chromatography ◽  
Maximal Activity ◽  
Thermophilic Bacterium ◽  
Single Band ◽  
Sds Page

AbstractObjective:In this study, α-amylase from a thermophilic bacterium Geobacillus sp. TF14 was purified and immobilized on two different supports.Methods:Ion exchange and hydrophobic interaction chromatography techniques were employed for the purification.Results:The enzyme was purified as 17.11 fold and determined as a single band of 54 kDa on SDS-PAGE. Purified enzyme showed two pH optimums of pH 5.00 and pH 9.00 and the enzyme is quite stable at these pHs over a period of 48 h. Purified enzyme showed maximal activity at 75°C and stability at this temperature over a period of 72 h. It was observed that CaConclusion:It can be concluded that the purified enzyme may find application in many fields of starch based industries.

Sign in / Sign up

Export Citation Format

Share Document