Lysine conjugation properties in human IgGs studied by integrating high‐resolution native mass spectrometry and bottom‐up proteomics

Publisher： John Wiley & Sons Inc

E-ISSN： 1615-9861|15|16|2756-2765

ISSN： 1615-9853

Source： PROTEOMICS, Vol.15, Iss.16, 2015-08, pp. : 2756-2765

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

Advances in high‐resolution accurate mass spectrometry application to targeted proteomics

By  

PROTEOMICS, Vol. 15, Iss. 5-6, 2015-03 ,pp. : 880-890

John Wiley & Sons Inc

Access to resources Recommend Favorite

Pitfalls in histone propionylation during bottom‐up mass spectrometry analysis

By  

PROTEOMICS, Vol. 15, Iss. 17, 2015-09 ,pp. : 2966-2971

John Wiley & Sons Inc

Access to resources Recommend Favorite

Comparative Proteomic Profile of the Human Umbilical Cord Blood Exosomes between Normal and Preeclampsia Pregnancies with High-Resolution Mass Spectrometry

By  

Cellular Physiology and Biochemistry, Vol. 36, Iss. 6, 2015-07 ,pp. : 2299-2306

Karger

Access to resources Recommend Favorite

Liquid chromatography high‐resolution mass spectrometry for fatty acid profiling

By  

THE PLANT JOURNAL, Vol. 81, Iss. 3, 2015-02 ,pp. : 529-536

John Wiley & Sons Inc

Access to resources Recommend Favorite

Native mass spectrometry and ion mobility characterization of trastuzumab emtansine, a lysine‐linked antibody drug conjugate

By  

PROTEIN SCIENCE (ELECTRONIC), Vol. 24, Iss. 8, 2015-08 ,pp. : 1210-1223

John Wiley & Sons Inc

Access to resources Recommend Favorite