Decoration of trastuzumab with short oligonucleotides: synthesis and detailed characterization

2017 ◽  
Vol 15 (42) ◽  
pp. 8923-8928 ◽  
Author(s):  
A. M. Carvalho ◽  
A. Manicardi ◽  
C. Véliz Montes ◽  
S. B. Gunnoo ◽  
R. J. Schneider ◽  
...  

Trastuzumab, an antibody prescribed for the treatment of metastatic breast cancer, was covalently conjugated to oligonucleotides and characterized by high resolution MALDI-ToF MS.

2013 ◽  
Vol 165 (3-4) ◽  
pp. 167-174 ◽  
Author(s):  
Maria Isabel Stets ◽  
Artur Soares Pinto ◽  
Luciano Fernandes Huergo ◽  
Emanuel Maltempi de Souza ◽  
Vandeir Francisco Guimarães ◽  
...  

PROTEOMICS ◽  
2008 ◽  
Vol 8 (8) ◽  
pp. 1530-1538 ◽  
Author(s):  
Maureen B. Tracy ◽  
Haijian Chen ◽  
Dennis M. Weaver ◽  
Dariya I. Malyarenko ◽  
Maciek Sasinowski ◽  
...  

2015 ◽  
Vol 50 (8) ◽  
pp. 1006-1012 ◽  
Author(s):  
Junji Mizukado ◽  
Hiroaki Sato ◽  
Liang Chen ◽  
Yasumasa Suzuki ◽  
Shogo Yamane ◽  
...  

1975 ◽  
Vol 21 (9) ◽  
pp. 1314-1322 ◽  
Author(s):  
John E Mrochek ◽  
Stanley R Dinsmore ◽  
T Phillip Waalkes

Abstract We describe a sensitive, reproducible procedure of analysis for the six neutral carbohydrates in glycoproteins, by high-resolution anion-exchange chromatography. As many as 16 neutral carbohydrates can be separated by elution with a concentration gradient of boric acid (pH 7, 67 to 672 mmol/liter). The carbohydrates are detected with a cerate oxidimetric detector system, which monitors the fluorescence of Ce3+ produced by the reaction of the eluted constituents with Ce4+. Sensitivity to 1 nmol of fucose is demonstrated. Analytical methods and results are presented for mannose, fucose, and galactose in serum glycoproteins of both normal women and those with metastatic breast cancer. We briefly discuss the possibility of separating and analyzing for the three neutral carbohydrates in serum glycoproteins in 4 h by isocratic (constant eluent concentration) elution from a chromatographic column.


2009 ◽  
Vol 27 (15_suppl) ◽  
pp. e22072-e22072
Author(s):  
D. Hawke ◽  
C. Mazouni ◽  
F. André ◽  
K. Baggerly ◽  
K. Baggerly ◽  
...  

e22072 Evaluation of serum profiles changes after neoadjuvant chemotherapy for breast cancer using MALDI-TOF / MS procedure. Background: Response to primary chemotherapy (CT) for breast cancer is heterogeneous among patients and a more tailored treatment would be beneficial in term of reducing exposure to an unnecessary toxicity and optimization of response rates. Mass spectrometry analysis of serum might be helpful in detecting specific changes in response to primary CT. Methods: An applied Biosystems 4700 Proteomics Analyzer matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer was used. A breast cancer cohort of 78 sera samples from 39 HER2 positive patients consisting of matched pretreatment and (6 months) posttreatment samples was used. Blood samples were collected serially before each treatment cycle every 3 weeks of neoadjuvant CT. Samples were divided into those who achieved pathological complete response (pCR, n= 20) and those who had residual disease (RD, n=19). Low-mass differentially expressed peptides were identified using MALDI-TOF/TOF. Results: This procedure yielded a total of 2329 and 3152 peaks respectively, for the responders and non-responders. Biological variation analysis revealed a total of 32 peaks for responders and 643 peaks for non-responders to be differentially regulated with a false discovery rate less than 20%. A total of 8 differentially expressed proteins were identified from their peptides after digestion and LC-MALDI-TOF/TOF. Four in tumors with pCR (AFM, C3, hemopexin, SAP) and four proteins in the RD group were identified (AP1, hemopexin, Complement B, amyloid P component) Conclusions: Our study suggests that MALDI mass spectrometry may be used to predict the tumor response to neoadjuvant chemotherapy. Proteomic analysis may be useful in developing tailored chemotherapy for breast cancer. No significant financial relationships to disclose.


2021 ◽  
Vol 17 (1) ◽  
Author(s):  
Aric J. McDaniel ◽  
Rachel J. Derscheid

Abstract Background Mycoplasma bovis is an important pathogen of cattle worldwide. Many different clinical manifestations of infection can occur, including respiratory disease, arthritis, and mastitis, causing heavy losses to beef and dairy industries. Because Mycoplasma species are slow-growing and fastidious, traditional identification methods are not cost- or time-effective, and improved methods are sought to streamline laboratory processes. High-resolution melting PCR (HRM-PCR) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) are 2 relatively recent tools that are rapid and inexpensive to use; we tested 9 isolates of M. bovis using both assays. The HRM-PCR assay used universal mycoplasma primers for the 16S–23S intergenic spacer region (IGSR). Results The resulting melting profiles of the field isolates were indistinguishable from the reference strain, indicating accurate identification. For the MALDI-TOF MS, each M. bovis isolate was accurately identified. Mycoplasma arginini and Mycoplasma alkalescens isolates did not identify as M. bovis when tested by either assay. Conclusions Our work shows that either assay could be used to identify unknown M. bovis isolates. For future work, the MALDI-TOF MS library should be expanded to include more mycoplasmas, and the HRM-PCR assay should be tested on additional mycoplasmas to ensure that the melting profiles are sufficiently distinctive.


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