Sucrose metabolism in cyanobacteria: sucrose synthase from Anabaena sp. strain PCC 7119 is remarkably different from the plant enzymes with respect to substrate affinity and amino-terminal sequence

Planta ◽  
1999 ◽  
Vol 210 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Andrea C. Porchia ◽  
Leonardo Curatti ◽  
Graciela L. Salerno
Keyword(s):  
Sucrose Synthase ◽  
Sucrose Metabolism ◽  
Substrate Affinity ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Plant Enzymes ◽  
Anabaena Sp ◽  
Amino Terminal Sequence

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

Prothrombin Fragment 1.2.3, A Major Product Of Prothrombin Activation In Human Plasma

1981 ◽  
Author(s):  
M J Rabiet ◽  
B Furie ◽  
B C Furie
Keyword(s):  
Sequence Analysis ◽  
Human Plasma ◽  
Gel Electrophoresis ◽  
Factor Xa ◽  
Normal Human Plasma ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Normal Human ◽  
Amino Terminal Sequence ◽  
Prothrombin Activation

The conversion of human prothrombin to thrombin is associated with a number of cleavage intermediates and products whose appearance and concentration are dependent upon the prothrombin activation conditions used. In the current investigation, the fragments of prothrombin which appear in normal human plasma after activation of the blood coagulation cascade were studied. Radioiodinated human prothrombin was added to platelet-poor relipidated normal human plasma and clotting initiated with Ca(II) and kaolin. The radiolabeled prothrombin cleavage products which formed were analyzed by polyacrylamide gel electrophoresis in the presence of dodecyl sulfate (SDS) and 2-mercaptoethanol (2-ME), A new product of prothrombin activation was observed. Its migration was more rapid than prethrombin 1 and slower than fragment 1.2. No previously identified products of prothrombin activation migrated to the same position in the gel.The previously unrecognized fragment was identified as fragment 1.2.3 as follows. Prothrombin was activated by factor Xa in the presence of Ca(II) and phospholipid. The desired product was isolated by absorption to and elution from barium citrate and by DEAE cellulose chromatography. This purified material, migrating identically with the unknown plasma product was homogeneous upon SDS gel electrophoresis with 2-ME. The amino terminal sequence of the isolated material was identical to that of prothrombin. Digestion of this material with either factor Xa or thrombin yielded as major products fragment 1.2 and fragment 1. (Fragment 2 and fragment 3 eluted from the gels under the conditions employed). Amino terminal sequence analysis of the factor Xa digestion products of the isolated material indicated three amino acid residues at each cycle. The sequences of fragment 1, fragment 2, and fragment 3 are consistent with this sequence analysis. On this basis we suggest that fragment 1.2.3 is a prominent product of prothrombin conversion to thrombin in plasma.

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