Recombinant Human Pancreatic Ribonuclease Produced in E. coli : Importance of the Amino-Terminal Sequence

1995 ◽  
Vol 216 (1) ◽  
pp. 406-413 ◽  
Author(s):  
J. Futami ◽  
M. Seno ◽  
M. Kosaka ◽  
H. Tada ◽  
S. Seno ◽  
...  
Keyword(s):  
Terminal Sequence ◽  
Pancreatic Ribonuclease ◽  
E Coli ◽  
Amino Terminal ◽  
Amino Terminal Sequence ◽  
Human Pancreatic Ribonuclease

Malate dehydrogenase: Isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms

1981 ◽  
Vol 1 (6) ◽  
pp. 497-507 ◽  
Author(s):  
Ross T. Fernley ◽  
Steven R. Lentz ◽  
Ralph A. Aradshaw
Keyword(s):  
Malate Dehydrogenase ◽  
Deae Cellulose ◽  
Mitochondrial Enzymes ◽  
Terminal Sequence ◽  
E Coli ◽  
Amino Terminal ◽  
Common Precursor ◽  
Polypeptide Chains ◽  
Mitochondrial Malate Dehydrogenase ◽  
Amino Terminal Sequence

Escherichia coli malate dehydrogenase has been isolated in homogeneous form by a procedure employing chromatography on DEAE-cellulose, 5′-AMP-Sepharose, and Sephacryl-200. It is composed of two identical polypeptide chains each of Mr = 32 500. Like porcine mitochondrial malate dehydrogenase, it is devoid of tryptophan, but otherwise it is not particularly more similar in composition to one of the eukaryotic isozymes than to the other. However, amino-terminal sequence analysis of the first 36 residues shows remarkable similarity of the bacterial and mitochondrial enzymes (69% identical residues) in contrast to the cytoplasmic form (27%). The two porcine heart enzymes are identical in 24t% of the positions compared. These results clearly establish that all three forms of malate dehydrogenase have evolved from a common precursor and that the prokaryotic and mitochondrial forms have retained sequences that are much closer to the ancestral one than the cytoplasmic enzyme. These findings appear to further substantiate the endosymbiotic hypothesis for the origin of the mitochondrion.

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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