γ-L-Glutamyl-L-cysteine: its isolation and identification from wheat germ

1977 ◽  
Vol 55 (4) ◽  
pp. 295-300 ◽  
Author(s):  
Russell Tkachuk ◽  
V. J. Mellish
Keyword(s):  
Amino Acid ◽  
Mass Spectroscopy ◽  
Amino Acid Analysis ◽  
Wheat Germ ◽  
Isolation And Identification

γ-L-Glutamyl-L-cysteine was isolated from wheat germ as the S-[2-14C]carboxymethyl derivative. Identity of the peptide was established by amino acid analysis, N-terminal procedures and mass spectroscopy.

L-Cysteinylglycine: its occurrence and identification

1970 ◽  
Vol 48 (9) ◽  
pp. 1029-1036 ◽  
Author(s):  
Russell Tkachuk
Keyword(s):  
Amino Acid ◽  
Human Serum ◽  
Mass Spectroscopy ◽  
Amino Acid Analysis ◽  
Wheat Germ ◽  
E Coli ◽  
Murine Tissue

L-Cysteinylglycine is present in wheat germ. The peptide was isolated as the S-carboxymethyl-2-14C derivative. The identity of S-carboxymethyl-L-cysteinylglycine was determined by amino acid analysis, N-terminal analysis, and mass spectroscopy. L-Cysteinylglycine appears to be widespread in nature as it is found also in E. coli, murine tissue, and human serum. It does not seem to be present in yeast.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

scholarly journals The Amino Acid Sequence of Wheat Germ Cytochrome c

1967 ◽  
Vol 242 (11) ◽  
pp. 2764-2779
Author(s):  
Frits C. Stevens ◽  
A.N. Glazer ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Wheat Germ

scholarly journals Whole-Genome Sequences of Influenza A(H1N1)pdm09 Virus Isolates from Kerala, India

2017 ◽  
Vol 5 (28) ◽  
Author(s):  
Sara Jones ◽  
Raji Prasad ◽  
Anjana S. Nair ◽  
Sanjai Dharmaseelan ◽  
Remya Usha ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Influenza A ◽  
Whole Genome Sequence ◽  
Whole Genome ◽  
H1n1 Pandemic ◽  
Genome Sequences ◽  
Influenza A H1n1 ◽  
Virus Isolates ◽  
New Mutations

ABSTRACT We report here the whole-genome sequence of six clinical isolates of influenza A(H1N1)pdm09, isolated from Kerala, India. Amino acid analysis of all gene segments from the A(H1N1)pdm09 isolates obtained in 2014 and 2015 identified several new mutations compared to the 2009 A(H1N1) pandemic strain.

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