scholarly journals Beta-succinyl-coenzyme A synthetase from Trichomonas vaginalis is a soluble hydrogenosomal protein with an amino-terminal sequence that resembles mitochondrial presequences.

1992 ◽  
Vol 174 (21) ◽  
pp. 6822-6830 ◽  
Author(s):  
C J Lahti ◽  
C E d'Oliveira ◽  
P J Johnson
Keyword(s):  
Trichomonas Vaginalis ◽  
Coenzyme A ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence ◽  
Succinyl Coenzyme A Synthetase

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.

The amino-terminal sequence of the VHIII subgroup ofpooled porcine IgG

1975 ◽  
Vol 5 (6) ◽  
pp. 427-429 ◽  
Author(s):  
F. Franěk ◽  
R. L. Wasserman ◽  
J Novotn ◽  
J. M. Kehoe
Keyword(s):  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence
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