Variability in the length of the amino terminal sequence contributes to the capsid protein diversity among dasheen mosaic potyvirus isolates

1994 ◽  
Vol 136 (3-4) ◽  
pp. 407-413 ◽  
Author(s):  
S. S. Pappu ◽  
H. R. Pappu ◽  
R. Lastra ◽  
C. L. Niblett



1994 ◽  
Vol 75 (1) ◽  
pp. 239-242 ◽  
Author(s):  
S. S. Pappu ◽  
H. R. Pappu ◽  
E. P. Rybicki ◽  
C. L. Niblett


1959 ◽  
Vol 234 (5) ◽  
pp. 1108-1111
Author(s):  
Bo G. Malmström ◽  
J.R. Kimmel ◽  
Emil L. Smith




1978 ◽  
Vol 56 (9) ◽  
pp. 920-925 ◽  
Author(s):  
N. G. Seidah ◽  
R. Routhier ◽  
M. Caron ◽  
M. Chrétien ◽  
S. Demassieux ◽  
...  

In this paper, we present the amino-terminal sequence of rat tonin, an endopeptidase responsible for the conversion of angiotensinogen, the tetradecapeptide renin substrate, or angiotensin I to angiotensin II. It is shown that isoleucine and proline occupy the amino- and carboxy-terminal residues respectively. The N-terminal sequence analysis permitted the identification of 34 out of the first 40 residue s of the single polypeptide chain composed of 272 amino acids. The se results showed an extensive homology with the sequence of many serine proteases of the trypsin–chymotrypsin family. This information, coupled with the slow inhibition of tonin by diisopropylfluorophosphate, classified this enzyme as a selective endopeptidase of the active serine protease family.





FEBS Letters ◽  
1985 ◽  
Vol 193 (2) ◽  
pp. 208-210 ◽  
Author(s):  
John Lucas ◽  
Agnes Menschen ◽  
Fritz Lottspeich ◽  
Urs Voegeli ◽  
Thomas Boiler


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