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.

Carnivora: The Amino Acid Sequence of the Adult European Polecat (Mustela putorius, Mustelidae) Hemoglobins

1989 ◽  
Vol 44 (7) ◽  
pp. 817-824 ◽  
Author(s):  
Aftab Ahmed ◽  
Meeno Jahan ◽  
Gerhard Braunitzer ◽  
Helmut Pechlaner
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gas Phase ◽  
Primary Structure ◽  
Amino Acid Sequences ◽  
Mustela Putorius ◽  
Globin Chains ◽  
The Family ◽  
High Degree ◽  
Β Chain

The complete amino acid sequences of the hemoglobins from the adult European polecat (Mustela putorius) are presented. The erythrocytes contain two hemoglobin components and three globin chains (α I, α II and β). The primary structure of globin chains and of the tryptic peptides determined in liquid- and gas-phase sequantors. Comparing the sequences of the globin chains of the polecat with that of human Hb-A, 17 (23.9%) substitutions were recognized in the α I, 16 (22.5%) in the α II and 14 (20.4%) in the β chain. A high degree of homology observed with other representatives of the family Mustelidae.

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

Crotalase and Thrombin: Cohomology of Amino Acid Sequences as Evidence for a Common Ancestral Gene

1979 ◽  
Author(s):  
Hubert Pirkle ◽  
Francis S. Markland ◽  
Ida Theodor ◽  
Richard Baumgartner
Keyword(s):  
Amino Acid ◽  
Mathematical Formulation ◽  
Evolutionary Relationship ◽  
Factor Xa ◽  
Amino Acid Sequences ◽  
Terminal Sequence ◽  
Ancestral Gene ◽  
Heavy Chains ◽  
Factor Ixa

Crotalase is a coagulant eniyme from the venom of C. adamanteus which releases specifically fibrinopeptide A from fibrinogen and cleaves the single thrombin-vulnerable bond of prothrombin. Edman degradation of crotalase yielded a six-step N-terminal sequence which contained only one residue in common with the N-terminal sequence of the B-chain of thrombin (Magnussen; Thompson et al.). When the two sequences were compared with the N-terminal sequences of the heavy chains of factor IXa (Enfield) and factor Xa (Titani), extensive identity was noted in five of the six positions, indicating evolutionary relationship among the four proteins and the suitability of the crotalase molecule for structure-function studies of thrombin-like actions. Our method for demonstrating that crotalase and thrombin are evolutionarily related is novel and is termed cohomology. We regard two amino acid sequences to be cohomologous when they each exhibit appreciable similarity to one or more di’ferent sequences but not to each other. We have found that this approach to the determination of evolutionary relationship, while employed intuitively here, is amenable to rigorous mathematical formulation (to be published).

Amino acid sequence of penicillopepsin. II. Isolation and characterization of thermolytic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 885-894 ◽  
Author(s):  
Leticia Rao ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Amino Acid Sequences ◽  
Porcine Pepsin ◽  
Isolation And Characterization

The determination of the amino acid sequences of 70 peptides obtained from a thermoiytic digest of penicillopepsin (EC 3.4.23.7) is described. Fifty-six unique sequences ranging from 2 to 13 amino acids were compiled. Among these was a heptapeptide whose sequence is nearly identical with that of the epoxide-reactive active site peptide of porcine pepsin (EC 3.4.23.1). Considering unrecognized overlaps, a minimum of 272 and a maximum of 293 unique amino acids have been obtained. They account for about 90% of the amino acids of the enzyme.

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