Amino acid analysis of spider dragline silk using 1H NMR

2013 ◽  
Vol 440 (2) ◽  
pp. 150-157 ◽  
Author(s):  
Xiangyan Shi ◽  
Gregory P. Holland ◽  
Jeffery L. Yarger
PLoS ONE ◽  
2017 ◽  
Vol 12 (8) ◽  
pp. e0183397 ◽  
Author(s):  
Ali D. Malay ◽  
Kazuharu Arakawa ◽  
Keiji Numata

2016 ◽  
Vol 46 (6) ◽  
pp. 552-558 ◽  
Author(s):  
Haibo Zhang ◽  
Fengli Zhou ◽  
Xinglin Jiang ◽  
Mingle Cao ◽  
Shilu Wang ◽  
...  

Evolution ◽  
2006 ◽  
Vol 60 (12) ◽  
pp. 2539 ◽  
Author(s):  
Brook O. Swanson ◽  
Todd A. Blackledge ◽  
Adam P. Summers ◽  
Cheryl Y. Hayashi

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček

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.


Author(s):  
Lizhong Dong ◽  
Jian Qiao ◽  
Yulong Wu ◽  
Ming Ren ◽  
Yulian Wang ◽  
...  

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