scholarly journals The amino-terminal sequence of the Xenopus laevis mitochondrial SSB is homologous to that of the Escherichia coli protein

FEBS Letters ◽  
1988 ◽  
Vol 235 (1-2) ◽  
pp. 267-270 ◽  
Author(s):  
C. Mahoungou ◽  
R. Ghrir ◽  
J.P. Lecaer ◽  
B. Mignotte ◽  
M. Barat-Gueride
Keyword(s):  
Escherichia Coli ◽  
Xenopus Laevis ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence

Sequence analysis of the heat-labile enterotoxin subunit B gene originating in human enterotoxigenic Escherichia coli

1982 ◽  
Vol 152 (1) ◽  
pp. 506-509
Author(s):  
T Yamamoto ◽  
T Tamura ◽  
M Ryoji ◽  
A Kaji ◽  
T Yokota ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Sequence ◽  
Enterotoxigenic Escherichia Coli ◽  
Mature Peptide ◽  
Terminal Sequence ◽  
E Coli ◽  
Amino Terminal ◽  
Heat Labile ◽  
Subunit B ◽  
Amino Terminal Sequence

In this study, we determined the amino-terminal coding sequence, covering the signal peptide and the amino-terminus of the mature peptide, of the heat-labile enterotoxin subunit B (LT-B) gene originating in human enterotoxigenic Escherichia coli. Neither the signal sequence nor the amino-terminal sequence of the mature LT-B was identical to those sequences from porcine enterotoxigenic E. coli, but there was an extensive homology.

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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