Synthesis and mass spectrometric identification of the major amino acid adducts formed between sulphur mustard and haemoglobin in human blood

1997 ◽  
Vol 71 (3) ◽  
pp. 171-178 ◽  
Author(s):  
Daan Noort ◽  
Albert G. Hulst ◽  
H. C. Trap ◽  
Leo P. A. de Jong ◽  
Hendrik P. Benschop
Keyword(s):  
Amino Acid ◽  
Human Blood ◽  
Mass Spectrometric ◽  
Sulphur Mustard ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification ◽  
Major Amino Acid

scholarly journals Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants

2019 ◽  
Vol 20 (11) ◽  
pp. 2633 ◽  
Author(s):  
Alexander Dergalev ◽  
Alexander Alexandrov ◽  
Roman Ivannikov ◽  
Michael Ter-Avanesyan ◽  
Vitaly Kushnirov
Keyword(s):  
Amino Acid ◽  
Ex Vivo ◽  
Mass Spectrometric ◽  
Proteinase K ◽  
Amino Acid Residues ◽  
Structural Variants ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification ◽  
Nonsense Suppressor ◽  
Different Origin

The yeast [PSI+] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differing in the strength of nonsense suppressor phenotype. Structure of [PSI+] and its variation are characterized poorly. Here, we mapped Sup35 amyloid cores of 26 [PSI+] ex vivo prions of different origin using proteinase K digestion and mass spectrometric identification of resistant peptides. In all [PSI+] variants the Sup35 amino acid residues 2–32 were fully resistant and the region up to residue 72 was partially resistant. Proteinase K-resistant structures were also found within regions 73–124, 125–153, and 154–221, but their presence differed between [PSI+] isolates. Two distinct digestion patterns were observed for region 2–72, which always correlated with the “strong” and “weak” [PSI+] nonsense suppressor phenotypes. Also, all [PSI+] with a weak pattern were eliminated by multicopy HSP104 gene and were not toxic when combined with multicopy SUP35. [PSI+] with a strong pattern showed opposite properties, being resistant to multicopy HSP104 and lethal with multicopy SUP35. Thus, Sup35 prion cores can be composed of up to four elements. [PSI+] variants can be divided into two classes reliably distinguishable basing on structure of the first element and the described assays.

Mass spectrometric identification of amino acid thiohydantoins

1976 ◽  
Vol 11 (6) ◽  
pp. 557-568 ◽  
Author(s):  
Tateo Suzuki ◽  
Kyung-Duck Song ◽  
Yasuhiro Itagaki ◽  
Katura Tuzimura
Keyword(s):  
Amino Acid ◽  
Mass Spectrometric ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification

Mass spectrometric identification of posttranslational modifications in transthyretin from human blood

2013 ◽  
Vol 47 (6) ◽  
pp. 885-893 ◽  
Author(s):  
I. A. Popov ◽  
N. L. Starodubtseva ◽  
M. I. Indeikina ◽  
Yu. I. Kostyukevich ◽  
A. S. Kononikhin ◽  
...  
Keyword(s):  
Human Blood ◽  
Posttranslational Modifications ◽  
Mass Spectrometric ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification

scholarly journals Mass Spectrometric Identification of Increased C16 Ceramide Levels During Apoptosis

1999 ◽  
Vol 274 (43) ◽  
pp. 30580-30588 ◽  
Author(s):  
Rexford L. Thomas ◽  
Christopher M. Matsko ◽  
Michael T. Lotze ◽  
Andrew A. Amoscato
Keyword(s):  
Mass Spectrometric ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification

scholarly journals Online H/D exchange liquid chromatography as a support for the mass spectrometric identification of the oxidation products of melatonin

2009 ◽  
Vol 44 (3) ◽  
pp. 318-329 ◽  
Author(s):  
Fabrice Collin ◽  
Dominique Bonnefont-Rousselot ◽  
Saï Yous ◽  
Catherine Marchetti ◽  
Daniel Jore ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Mass Spectrometric ◽  
Oxidation Products ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification
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