scholarly journals Molecular characterization of human Ro/SS-A antigen. Amino terminal sequence of the protein moiety of human Ro/SS-A antigen and immunological activity of a corresponding synthetic peptide.

1988 ◽  
Vol 82 (1) ◽  
pp. 96-101 ◽  
Author(s):  
T S Lieu ◽  
M M Newkirk ◽  
J D Capra ◽  
R D Sontheimer
Keyword(s):  
Molecular Characterization ◽  
Synthetic Peptide ◽  
Terminal Sequence ◽  
Immunological Activity ◽  
Amino Terminal ◽  
Amino Terminal Sequence ◽  
Protein Moiety

scholarly journals Characterization of a Granulovirus Isolated from Epinotia aporema Wals. (Lepidoptera: Tortricidae) Larvae

2001 ◽  
Vol 67 (8) ◽  
pp. 3702-3706 ◽  
Author(s):  
Alicia Sciocco-Cap ◽  
Alejandro D. Parola ◽  
Alina V. Goldberg ◽  
Pablo D. Ghiringhelli ◽  
Vı́ctor Romanowski
Keyword(s):  
Biological Control ◽  
High Specificity ◽  
Biological Properties ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Soybean Pest ◽  
Occlusion Bodies ◽  
Amino Terminal Sequence ◽  
Epinotia Aporema

ABSTRACT A granulovirus (GV) isolated from Epinotia aporema(Lepidoptera: Tortricidae)—a major soybean pest—was studied in terms of its main morphological, biochemical, and biological properties. The ovoidal occlusion bodies were 466 by 296 nm in size, and their most prominent protein had an apparent molecular mass of 29 kDa. Its amino-terminal sequence was remarkably homologous to that of the granulins of other GVs. The DNA genome size was estimated to be 120 kbp. The high specificity and pathogenicity of this newly described granulovirus (EpapGV) indicate that it is indeed a good candidate for the biological control of this pest.

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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