Amino-terminal sequence of the 21 kDa apoprotein of a minor light- harvesting pigment-protein complex of the Photosystem II antenna (LHC IId/CP24)

FEBS Letters ◽  
1990 ◽  
Vol 264 (2) ◽  
pp. 239-242 ◽  
Author(s):  
Daryl T. Morishige ◽  
Shivanthi Anandan ◽  
James T. Jaing ◽  
J.Philip Thornber
Keyword(s):  
Photosystem Ii ◽  
Protein Complex ◽  
Light Harvesting ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
A Minor ◽  
Pigment Protein Complex ◽  
Amino Terminal Sequence

N-Terminal amino acid sequence of rat tonin: homology with serine proteases

1978 ◽  
Vol 56 (9) ◽  
pp. 920-925 ◽  
Author(s):  
N. G. Seidah ◽  
R. Routhier ◽  
M. Caron ◽  
M. Chrétien ◽  
S. Demassieux ◽  
...  
Keyword(s):  
Serine Proteases ◽  
Terminal Sequence ◽  
Renin Substrate ◽  
Amino Terminal ◽  
Single Polypeptide Chain ◽  
Serine Protease Family ◽  
Terminal Amino ◽  
Single Polypeptide ◽  
Carboxy Terminal ◽  
Amino Terminal Sequence

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.

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