The amino-terminal sequence of the heavy chain of human immunoglobulin M

Biochemistry ◽  
1968 ◽  
Vol 7 (10) ◽  
pp. 3340-3344 ◽  
Author(s):  
J. Claude. Bennett
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin M ◽  
Human Immunoglobulin ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence

scholarly journals Antiplasmin, the Fast-Reacting Plasmin Inhibitor of Human Plasma

1977 ◽  
Author(s):  
D. Collen ◽  
B. Wiman
Keyword(s):  
Human Plasma ◽  
Heavy Chain ◽  
Light Chain ◽  
Concanavalin A ◽  
Active Site ◽  
Gel Electrophoresis ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence ◽  
Plasmin Inhibitor

Recently a new plasmin inhibitor was discovered in human plasma by three different groups (Eur. J. Biochem. 69, 209, 1976; J. Biol. Chem. 251, 5956, 1976; Biochem. J. 159, 545, 1976). This inhibitor is responsible for the fast-reacting plasmin-neutraIizing activity of human plasma and forms a very stable 1:1 molar complex with plasmin, which is devoid of protease and esterase activity. The concentration of antiplasmin in human plasma is approximately I μM (2/3 that of plasminogen).We have purified the inhibitor by affinity chromatography on insolubilized plasminogen, followed by DEAE-Sephadex and concanavalin A chromatography. It is a glycoprotein with a mol . wt. of 67,000 (SDS-gel electrophoresis), a carbohydrate content of 14%, and amino terminal sequence Asn-Gln-Glu-Gly (Wiman and Collen, submitted).The inhibitor interacts strongly with the light chain of plasmin (probably through reaction with the active site serine), and weakly with the heavy chain (probably through interaction with the lysine-binding site), suggesting that antiplasmin not only functions as an inhibitor of plasmin, but also interferes with the interaction between plasm in (ogen) and fibrin.

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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