The Primary Structure of Proteins. Principles and Practices for the Determination of Amino Acid Sequence.Walter A. Schroeder

1969 ◽  
Vol 44 (3) ◽  
pp. 300-301
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Structure Of Proteins

Determination of Factor Xa Activity by Means of Chromogenic Substrates Based on the Primary Structure of Prothrombin

1975 ◽  
Author(s):  
L. Aurell ◽  
A. Olausson ◽  
G. Claeson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Serine Proteases ◽  
Factor Xa ◽  
Amino Acid Sequences ◽  
Peptide Substrate ◽  
Chromogenic Substrates ◽  
Special Regard

Through the work of Magnusson and co-workers leading to the elucidation of the primary structure of prothrombin including the amino acid sequences around the two bonds split by factor Xa it has been possible to design a synthetic chromogenic peptide substrate. Bz-Ile-Glu-Gly-Arg-pNA, specifically intended for the determination of factor Xa. Furthermore, additional substrates have been synthezised with various alterations in the amino acid sequence. The activity of factor Xa and other serine proteases within the coagulation and fibrinolytic systems towards these substrates will be discussed with special regard to their possible use in coagulation studies.

scholarly journals Primary structure of hemoglobins from trout(Salmo irideus). Partial determination of amino acid sequence of Hb trout IV

FEBS Letters ◽  
1976 ◽  
Vol 64 (1) ◽  
pp. 76-80 ◽  
Author(s):  
F. Bossa ◽  
D. Barra ◽  
M. Coletta ◽  
F. Martini ◽  
A. Liverzani ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure

scholarly journals Primary structure of porcine spleen ribonuclease: sequence homology.

1997 ◽  
Vol 44 (4) ◽  
pp. 689-699 ◽  
Author(s):  
A Kusano ◽  
M Iwama ◽  
A Sanda ◽  
K Suwa ◽  
E Nakaizumi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Gel Filtration ◽  
Animal Origin ◽  
Amino Acid Residues ◽  
Function Relationship ◽  
Rnase T2 ◽  
Relationship Of ◽  
Protein Moiety

The primary structure of porcine spleen RNase (RNase Psp1) was investigated as a mean of assessing the structure-function relationship of base non-specific ribonucleases of animal origin. N-terminal analysis of RNase Psp1 yielded three N-terminal sequences. These peptides were separated by gel-filtration on Superdex 75HR, after reduction and S-carboxymethylation of RNase Psp1. Determination of the amino-acid sequence of these peptides indicated that the RNase Psp1 preparation consisted of three peptides having 20 (RCM RNase Psp1 pep1), 15 (RCM RNase Psp1 pep2), and 164 (RCM RNase Psp1 pro) amino-acid residues, respectively. It possessed two unique segments containing most of the active site amino-acid residues of the RNases of the RNase T2 family. The alignment of these three peptides in RNase Psp1 was determined by comparison with the other enzymes in the RNase T2 family. The overall results showed that RCM RNase Psp1 pep1 and RCM RNase Psp1 pep2 are derived from the N-terminal and C-terminal regions of RNase Psp1, respectively, probably by processing by some protease. The molecular mass of the protein moiety of RNase Psp1 was 23235 Da.

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