The Mode of Action of Thrombin

SummaryThe peptides liberated from fibrinogen by the action of thrombin have been isolated on modified cellulose adsorbents. These peptides have been characterized by sedimentation-diffusion measurements by quantitative amino acid analysis, and by C-terminal analysis. Both peptides were found to contain arginine as C-terminal amino acid. Thrombin thus splits specific arginyl-glycine bonds in the fibrinogen molecule. The specificity of thrombin is discussed in view of the finding that the active center of thrombin is similar to that of trypsin and chymotrypsin.

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Existence of Common Antigenic Determinants in the Aα, Bβ and γ Chains of Some Mammalian Fibrinogens.

10.1055/s-0039-1687463 ◽

1979 ◽

Author(s):

C.S. Cierniewski

Keyword(s):

Amino Acid ◽

Polyacrylamide Gel Electrophoresis ◽

Polyacrylamide Gel ◽

Antigenic Determinants ◽

Terminal Amino Acid ◽

Human Fibrinogen ◽

Passive Hemagglutination ◽

Terminal Amino ◽

Polypeptide Chains ◽

Fibrinogen Molecule

Polypeptide chains Aα, Bβ and γ of porcine fibrinogen were isolated by preparative SDS polyacrylamide gel electrophoresis. Their purity was estimated by electrophoresis in polyacrylamide gel, amino acid composition and N-terminal amino acid analyses. Antisera to the pig polypeptide chains were produced in rabbits and they were employed in immunological comparative studies of porcine, bovine, human and duck fibrinogens. Antisera to the pig Aα chain showed in gel immunodiffusion and passive hemagglutination a strong cross-reaction with porcine, bovine and human fibrinogens. Antisera to the pig βB and γ chains cross-reacted only with porcine and bovine fibrinogens but they did not recognize human fibrinogen, The reaction of antiγ antisera was detectable only by passive hemagglutination test. In all cases antigenic similarity of the analyzed fibrinogens was mainly related to antigenic determinants of the Aα, Bβ and γ chains exposed on the intact fibrinogen molecule. None of analyzed antisera reacted with duck fibrinogen.

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Human fibroblast interferon: amino acid analysis and amino terminal amino acid sequence

Science ◽

10.1126/science.7352259 ◽

1980 ◽

Vol 207 (4430) ◽

pp. 525-526 ◽

Cited By ~ 128

Author(s):

E Knight ◽

M. Hunkapiller ◽

B. Korant ◽

R. Hardy ◽

L. Hood

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Human Fibroblast ◽

Amino Acid Analysis ◽

Terminal Amino Acid ◽

Amino Terminal ◽

Terminal Amino ◽

Terminal Amino Acid Sequence

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N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/0005-2736(73)90246-0 ◽

1973 ◽

Vol 330 (3) ◽

pp. 356-361 ◽

Cited By ~ 47

Author(s):

Hubertus Knufermann ◽

Sucharit Bhakdi ◽

R. Schmidt-Ullrich ◽

Donald F. Hoelzl Wallach

Keyword(s):

Amino Acid ◽

Amino Acid Analysis ◽

Erythrocyte Ghosts ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Protein Components

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Purification, N-terminal amino acid analysis, and disruption of an influenza virus

Virology ◽

10.1016/0042-6822(61)90348-8 ◽

1961 ◽

Vol 14 (4) ◽

pp. 499-502 ◽

Cited By ~ 16

Author(s):

W.G. Laver

Keyword(s):

Influenza Virus ◽

Amino Acid ◽

Amino Acid Analysis ◽

Terminal Amino Acid ◽

Terminal Amino

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Terminal Amino-Acid Analysis of Vasculokinase-activated Fibrin

Nature ◽

10.1038/194681a0 ◽

1962 ◽

Vol 194 (4829) ◽

pp. 681-681 ◽

Cited By ~ 5

Author(s):

MARVIN MURRAY ◽

LAMAN GRAY

Keyword(s):

Amino Acid ◽

Amino Acid Analysis ◽

Terminal Amino Acid ◽

Terminal Amino

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Application of a microbore high-performance liquid chromatography—chemiluminescence detection system to the N-terminal amino acid analysis of bradykinin

Journal of Chromatography A ◽

10.1016/s0021-9673(01)83384-7 ◽

1986 ◽

Vol 352 ◽

pp. 255-260 ◽

Cited By ~ 28

Author(s):

Kimitoshi Miyaguchi ◽

Kazumasa Honda ◽

Toshimasa Toyo'oka ◽

Kazuhiro Imai

Keyword(s):

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

Amino Acid ◽

Amino Acid Analysis ◽

High Performance ◽

Detection System ◽

Chemiluminescence Detection ◽

Terminal Amino Acid ◽

Terminal Amino

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Human hemopexin. Preparation of the heme-rich protein

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19820535 ◽

1982 ◽

Vol 47 (2) ◽

pp. 535-542 ◽

Cited By ~ 2

Author(s):

Ladislav Morávek ◽

Josef Borvák ◽

Karel Grüner ◽

Bedřich Meloun ◽

Petr Štrop ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Amino Acid Analysis ◽

Gel Filtration ◽

Deae Cellulose ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Simplified Procedure ◽

Pooled Samples ◽

Terminal Amino Acid Sequence

A simplified procedure was developed for the preparation of hemopexin from Cohn fraction IV obtained from partially hemolyzed pooled samples of serum. The method is based on precipitation with rivanol, chromatography on DEAE-cellulose, and gel filtration; it permits large quantities of the material to be treated on a laboratory scale. The preparation of heme-rich hemopexin obtained was characterized by amino acid analysis and the following N-terminal amino acid sequence: Thr-Pro-Leu-Pro-Arg-Gly-Ser-Ala-His-Gly-Asn-Val-Ala-Glu-Gly-Glu-Thr(Thr)Thr-Asn-Pro-Asp-Val-(Gly)(Leu).

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