Rapid mass-spectrometric identification of the N-terminal amino-acid residue in terminal N-thiobenzoyl polypeptides

1968 ◽  
pp. 335
Author(s):  
G. C. Barrett ◽  
J. R. Chapman
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Mass Spectrometric ◽  
Terminal Amino Acid ◽  
Spectrometric Identification ◽  
Mass Spectrometric Identification ◽  
Terminal Amino ◽  
Rapid Mass

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.

Plasma Oxytocinase: The Synthesis and Biological Properties of the First Prodoct of the Degradation of Oxytocin by this Enzyme

1974 ◽  
Vol 52 (1) ◽  
pp. 60-66 ◽  
Author(s):  
B. M. Ferrier ◽  
J. M. Hendrie ◽  
L. A. Branda
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Pregnant Women ◽  
Amino Acid Residue ◽  
Biological Properties ◽  
Milk Ejection ◽  
Terminal Amino Acid ◽  
Molecular Features ◽  
Marked Inhibition ◽  
Terminal Amino

Oxytocin is hydrolytically cleaved in the presence of plasma oxytocinase to give an acyclic peptide, tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-(S-cysteine)-cysteinyl-prolyl-leucyl-glycinamide (1,2-acyclic oxytocin). The synthesis of this peptide is described. It is shown to be of very low potency in milk-ejection-like activity and uterotonic activity. It does not inhibit the expression of these activities by oxytocin, suggesting that it does not interfere with the hormone's binding to target tissues. The presence of 1,2-acyclic oxytocin slightly inhibits the rate of degradation of oxytocin by plasma from pregnant women, in contrast to the marked inhibition of the degradation of cystine di-β-naphthylamide. The Km for the degradation of oxytocin is 30 times smaller than that of the degradation of cystine di-β-naphthylamide, which is of the same order as the Ki for the inhibition of the degradation of cystine di-β-naphthylamide by 1,2-acyclic oxytocin. These results, together with information on the substrate specificity of plasma oxytocinase with respect to the N-terminal amino acid residue, suggest that there are molecular features of oxytocin other than its N-terminal residue that facilitate its interaction with plasma oxytocinase.

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

The degradation of glycoproteins with lithium borohydride: Isolation and analysis ofO-glycopeptides with reducedC-terminal amino acid residue

2000 ◽  
Vol 26 (1) ◽  
pp. 45-53
Author(s):  
N. P. Arbatsky ◽  
L. M. Likhosherstov ◽  
M. V. Serebryakova ◽  
O. S. Brusov ◽  
V. N. Shibaev ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Terminal Amino Acid ◽  
Lithium Borohydride ◽  
Terminal Amino

scholarly journals Significance of the C-terminal amino acid residue in mengovirus RNA-dependent RNA polymerase

Virology ◽  
2007 ◽  
Vol 365 (1) ◽  
pp. 79-91 ◽  
Author(s):  
Tatiana M. Dmitrieva ◽  
Andrei V. Alexeevski ◽  
Galina S. Shatskaya ◽  
Elena A. Tolskaya ◽  
Anatoly P. Gmyl ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rna Polymerase ◽  
Amino Acid Residue ◽  
Terminal Amino Acid ◽  
Rna Dependent Rna Polymerase ◽  
Terminal Amino
Sign in / Sign up

Export Citation Format

Share Document