Combination of SDS-PAGE and intact mass analysis for rapid determination of heterogeneities in monoclonal antibody therapeutics

2017 ◽  
Vol 38 (9-10) ◽  
pp. 1344-1352 ◽  
Author(s):  
Hideaki Yamada ◽  
Chiemi Matsumura ◽  
Keita Yamada ◽  
Koichiro Teshima ◽  
Takashi Hiroshima ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Rapid Determination ◽  
Mass Analysis ◽  
Antibody Therapeutics ◽  
Sds Page ◽  
Intact Mass

scholarly journals Charge variant native mass spectrometry benefits mass precision and dynamic range of monoclonal antibody intact mass analysis

mAbs ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 1214-1225 ◽  
Author(s):  
Aaron O. Bailey ◽  
Guanghui Han ◽  
Wilson Phung ◽  
Paul Gazis ◽  
Jennifer Sutton ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Monoclonal Antibody ◽  
Dynamic Range ◽  
Native Mass Spectrometry ◽  
Mass Analysis ◽  
Intact Mass

Weak Beam Imaging and Diffraction Studies of Stacking Faults in Silicon

1976 ◽  
Vol 34 ◽  
pp. 590-591
Author(s):  
T. Y. Tan ◽  
W. K. Tice
Keyword(s):  
Fast Neutron ◽  
Rapid Determination ◽  
Stacking Faults ◽  
Imaging Method ◽  
Large Reduction ◽  
Dislocation Loops ◽  
Fringe Spacing ◽  
Weak Beam ◽  
Kinematical Theory

In studying ion implanted semiconductors and fast neutron irradiated metals, the need for characterizing small dislocation loops having diameters of a few hundred angstrom units usually arises. The weak beam imaging method is a powerful technique for analyzing these loops. Because of the large reduction in stacking fault (SF) fringe spacing at large sg, this method allows for a rapid determination of whether the loop is faulted, and, hence, whether it is a perfect or a Frank partial loop. This method was first used by Bicknell to image small faulted loops in boron implanted silicon. He explained the fringe spacing by kinematical theory, i.e., ≃l/(Sg) in the fault fringe in depth oscillation. The fault image contrast formation mechanism is, however, really more complicated.

The Anticoagulant Properties of a Modified Form of Protein S

1988 ◽  
Vol 60 (02) ◽  
pp. 298-304 ◽  
Author(s):  
C A Mitchell ◽  
S M Kelemen ◽  
H H Salem
Keyword(s):  
Monoclonal Antibody ◽  
Anticoagulant Activity ◽  
Activated Protein C ◽  
Factor Xa ◽  
Protein S ◽  
Human Neutrophil Elastase ◽  
Factor X ◽  
Sds Page

SummaryProtein S (PS) is a vitamin K-dependent anticoagulant that acts as a cofactor to activated protein C (APC). To date PS has not been shown to possess anticoagulant activity in the absence of APC.In this study, we have developed monoclonal antibody to protein S and used to purify the protein to homogeneity from plasma. Affinity purified protein S (PSM), although identical to the conventionally purified protein as judged by SDS-PAGE, had significant anticoagulant activity in the absence of APC when measured in a factor Xa recalcification time. Using SDS-PAGE we have demonstrated that prothrombin cleavage by factor X awas inhibited in the presence of PSM. Kinetic analysis of the reaction revealed that PSM competitively inhibited factor X amediated cleavage of prothrombin. PS preincubated with the monoclonal antibody, acquired similar anticoagulant properties. These results suggest that the interaction of the monoclonal antibody with PS results in an alteration in the protein exposing sites that mediate the observed anticoagulant effect. Support that the protein was altered was derived from the observation that PSM was eight fold more sensitive to cleavage by thrombin and human neutrophil elastase than conventionally purified protein S.These observations suggest that PS can be modified in vitro to a protein with APC-independent anticoagulant activity and raise the possibility that a similar alteration could occur in vivo through the binding protein S to a cellular or plasma protein.

Methods for rapid determination of pecan (Carya illinoensis) seed viability

2017 ◽  
Vol 45 (2) ◽  
pp. 455-464
Author(s):  
T.T. Xue ◽  
J. Liu ◽  
Y.B. Shen ◽  
G.Q. Liu
Keyword(s):  
Rapid Determination ◽  
Seed Viability ◽  
Carya Illinoensis
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